CPAD 2.0

Entry	PDB ID	Protein Name	Species	Length	Mutation(s)	Class	Type	Method	Resolution (Å)	PMID
S-0241	3GPS	Transthyretin	Homo sapiens	127	F87M/L110M	Amyloid	Aggregating complex	X-RAY DIFFRACTION	1.78	20659897
S-0242	3GRB	Transthyretin	Homo sapiens	127	F87M/L110M	Amyloid	Aggregating complex	X-RAY DIFFRACTION	1.75	20659897
S-0243	3GRG	Transthyretin	Homo sapiens	127	F87M/L110M	Amyloid	Aggregating complex	X-RAY DIFFRACTION	1.9	20659897
S-0244	3GS0	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.85	19621084
S-0245	3GS4	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.78	19621084
S-0246	3GS7	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.8	19621084
S-0247	3HJ0	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.34	20081815
S-0248	3HYD	Insulin	Homo sapiens	7	No	Amyloid	Fibril	X-RAY DIFFRACTION	1.0	19864624
S-0249	3I9A	Transthyretin	Homo sapiens	127	No	Amyloid	Protein	X-RAY DIFFRACTION	1.65
S-0250	3I9I	Transthyretin	Homo sapiens	116	No	Amyloid	Protein	X-RAY DIFFRACTION	1.8
S-0251	3I9P	Transthyretin	Homo sapiens	116	No	Amyloid	Protein	X-RAY DIFFRACTION	1.9
S-0252	3IMR	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.7	20043671
S-0253	3IMS	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.4	20043671
S-0254	3IMT	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.4	20043671
S-0255	3IMU	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.4	20043671
S-0256	3IMV	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.47	20043671
S-0257	3IMW	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.31	20043671
S-0258	3IPB	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.9	21059958
S-0259	3IPE	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.4	21059958
S-0260	3JQ5	Amyloid-beta		119 , 8	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	2.03
S-0261	3KGS	Transthyretin	Homo sapiens	127	V30M	Amyloid	Protein	X-RAY DIFFRACTION	1.8	20211733
S-0262	3KGT	Transthyretin	Homo sapiens	127	V30M	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.95	20211733
S-0263	3KGU	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.85	20211733
S-0264	3LN9	B10 Antibody Fragment	Camelidae	139	No	Amyloid	Fibril complex	X-RAY DIFFRACTION	1.8	21059358
S-0265	3LOW	Beta-2-microglobulin	Homo sapiens	100	No	Amyloid	Protein	X-RAY DIFFRACTION	2.3	21131979
S-0266	3LOZ	Beta-2-microglobulin	Homo sapiens	6	No	Amyloid	Fibril	X-RAY DIFFRACTION	1.8	21131979
S-0267	3M1O	Transthyretin	Homo sapiens	127	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.2	21059958
S-0268	3MOQ	Amyloid beta		126	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	2.05	21273426
S-0269	3NA4	Beta-2-microglobulin	Homo sapiens	100	D53P	Amyloid	Protein	X-RAY DIFFRACTION	1.9	21569201
S-0270	3NEE	Transthyretin	Homo sapiens	116	No	Non-amyloid	Inhibitor complex	X-RAY DIFFRACTION	1.55	20937391

Structure

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View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 3

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 4

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Crystal structure of the F87M/L110M mutant of human transthyretin at pH 5.5

They report the first crystal structure of human TTR in complex with Zn(2+) at pH 4.6-7.5. All four structures reveal three tetra-coordinated Zn(2+)-binding sites (ZBS 1-3) per monomer, plus a fourth site (ZBS 4) involving amino acid residues from a symmetry-related tetramer that is not visible in solution by NMR. Stability of the monomer of TTR decreases in the presence of Zn(2+), which is consistent with the tertiary structural perturbation provoked by Zn(2+) binding, tetramer stability is only marginally affected by Zn(2+). These data highlight structural and functional roles of Zn(2+) in TTR-related amyloidoses.

Literature

PMID:	20659897
Author(s):	Palmieri, L.de.C., Lima, L.M., Freire, J.B., Bleicher, L., Polikarpov, I., Almeida, F.C., Foguel, D.
Reference:	J Biol Chem. 2010 Oct 8;285(41):31731-41.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	F87M/L110M
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3GPS
Amyloid Category:	Amyloid
Type:	Aggregating complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	TRANSPORT PROTEIN
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.78
R free:	0.254

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
ACT	A	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	A	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	A	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACT	B	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	B	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	B	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACT	C	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	C	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	C	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACT	D	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	D	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	D	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 3

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 4

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Crystal structure of the F87M/L110M mutant of human transthyretin at pH 6.5

They report the first crystal structure of human TTR in complex with Zn(2+) at pH 4.6-7.5. All four structures reveal three tetra-coordinated Zn(2+)-binding sites (ZBS 1-3) per monomer, plus a fourth site (ZBS 4) involving amino acid residues from a symmetry-related tetramer that is not visible in solution by NMR. Stability of the monomer of TTR decreases in the presence of Zn(2+), which is consistent with the tertiary structural perturbation provoked by Zn(2+) binding, tetramer stability is only marginally affected by Zn(2+). These data highlight structural and functional roles of Zn(2+) in TTR-related amyloidoses.

Literature

PMID:	20659897
Author(s):	Palmieri, L.de.C., Lima, L.M., Freire, J.B., Bleicher, L., Polikarpov, I., Almeida, F.C., Foguel, D.
Reference:	J Biol Chem. 2010 Oct 8;285(41):31731-41.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	F87M/L110M
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3GRB
Amyloid Category:	Amyloid
Type:	Aggregating complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	TRANSPORT PROTEIN
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.75
R free:	0.26

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
GOL	A	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	A	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACT	B	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	B	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	B	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACT	C	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	C	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	C	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACT	D	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	D	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	D	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 3

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 4

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

M

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

M

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Crystal structure of the F87M/L110M mutant of human transthyretin at pH 7.5

They report the first crystal structure of human TTR in complex with Zn(2+) at pH 4.6-7.5. All four structures reveal three tetra-coordinated Zn(2+)-binding sites (ZBS 1-3) per monomer, plus a fourth site (ZBS 4) involving amino acid residues from a symmetry-related tetramer that is not visible in solution by NMR. Stability of the monomer of TTR decreases in the presence of Zn(2+), which is consistent with the tertiary structural perturbation provoked by Zn(2+) binding, tetramer stability is only marginally affected by Zn(2+). These data highlight structural and functional roles of Zn(2+) in TTR-related amyloidoses.

Literature

PMID:	20659897
Author(s):	Palmieri, L.de.C., Lima, L.M., Freire, J.B., Bleicher, L., Polikarpov, I., Almeida, F.C., Foguel, D.
Reference:	J Biol Chem. 2010 Oct 8;285(41):31731-41.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	F87M/L110M
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3GRG
Amyloid Category:	Amyloid
Type:	Aggregating complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	TRANSPORT PROTEIN
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.9
R free:	0.255

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
ACT	A	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	A	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	A	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACT	B	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	B	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	B	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACT	C	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
ZN	C	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N
ACT	D	C2 H3 O2 -1	59.04	ACETATE ION	CC(=O)[O-]	QTBSBXVTEAMEQO-UHFFFAOYSA-M
GOL	D	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
ZN	D	Zn 2	65.41	ZINC ION	[Zn+2]	PTFCDOFLOPIGGS-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Human transthyretin (TTR) complexed with (S)-3-(9H-fluoren-9-ylideneaminooxy)-2-methylpropanoic acid (inhibitor 16) 69% inhibition

TTR amyloidogenesis can be inhibited through stabilization of the native tetramer state by small molecule binding to the thyroid hormone sites of TTR. They have evaluated a new series of Beta-aminoxypropionic acids (compounds 5-21), with a single aromatic moiety (aryl or fluorenyl) linked through a flexible oxime tether to a carboxylic acid. These compounds are structurally distinct from the native ligand thyroxine and typical halogenated biaryl NSAID-like inhibitors to avoid off-target hormonal or anti-inflammatory activity.

Literature

PMID:	19621084
Author(s):	Palaninathan, S.K., Mohamedmohaideen, N.N., Orlandini, E., Ortore, G., Nencetti, S., Lapucci, A., Rossello, A., Freundlich, J.S., Sacchettini, J.C.
Reference:	PLoS One. 2009 Jul 21;4(7):e6290.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3GS0
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 2-mer - A2
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.85
R free:	0.26899999

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
6BD	A	C17 H15 N O3	281.31	(2S)-3-[(9H-fluoren-9-ylideneamino)oxy]-2-methylpropanoic acid	C[C@@H](CON=C1c2ccccc2-c3c1cccc3)C(=O)O	ZHFDVDMCVXUGGF-NSHDSACASA-N
6BD	B	C17 H15 N O3	281.31	(2S)-3-[(9H-fluoren-9-ylideneamino)oxy]-2-methylpropanoic acid	C[C@@H](CON=C1c2ccccc2-c3c1cccc3)C(=O)O	ZHFDVDMCVXUGGF-NSHDSACASA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Human transthyretin (TTR) complexed with 3-(9H-fluoren-9-ylideneaminooxy)propanoic acid (inhibitor 15) 69% inhibition

TTR amyloidogenesis can be inhibited through stabilization of the native tetramer state by small molecule binding to the thyroid hormone sites of TTR. They have evaluated a new series of Beta-aminoxypropionic acids (compounds 5-21), with a single aromatic moiety (aryl or fluorenyl) linked through a flexible oxime tether to a carboxylic acid. These compounds are structurally distinct from the native ligand thyroxine and typical halogenated biaryl NSAID-like inhibitors to avoid off-target hormonal or anti-inflammatory activity.

Literature

PMID:	19621084
Author(s):	Palaninathan, S.K., Mohamedmohaideen, N.N., Orlandini, E., Ortore, G., Nencetti, S., Lapucci, A., Rossello, A., Freundlich, J.S., Sacchettini, J.C.
Reference:	PLoS One. 2009 Jul 21;4(7):e6290.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3GS4
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 2-mer - A2
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.78
R free:	0.278

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
7BD	A	C16 H13 N O3	267.28	3-[(9H-fluoren-9-ylideneamino)oxy]propanoic acid	c1ccc2c(c1)-c3ccccc3C2=NOCCC(=O)O	LASWLEUVWJDDBA-UHFFFAOYSA-N
7BD	B	C16 H13 N O3	267.28	3-[(9H-fluoren-9-ylideneamino)oxy]propanoic acid	c1ccc2c(c1)-c3ccccc3C2=NOCCC(=O)O	LASWLEUVWJDDBA-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Human transthyretin (TTR) complexed with (E)-3-(2-methoxybenzylideneaminooxy)propanoic acid (inhibitor 13) 51% inhibition

TTR amyloidogenesis can be inhibited through stabilization of the native tetramer state by small molecule binding to the thyroid hormone sites of TTR. They have evaluated a new series of Beta-aminoxypropionic acids (compounds 5-21), with a single aromatic moiety (aryl or fluorenyl) linked through a flexible oxime tether to a carboxylic acid. These compounds are structurally distinct from the native ligand thyroxine and typical halogenated biaryl NSAID-like inhibitors to avoid off-target hormonal or anti-inflammatory activity.

Literature

PMID:	19621084
Author(s):	Palaninathan, S.K., Mohamedmohaideen, N.N., Orlandini, E., Ortore, G., Nencetti, S., Lapucci, A., Rossello, A., Freundlich, J.S., Sacchettini, J.C.
Reference:	PLoS One. 2009 Jul 21;4(7):e6290.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3GS7
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 2-mer - A2
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.8
R free:	0.266

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
8BD	A	C11 H13 N O4	223.23	3-({[(1Z)-(2-methoxyphenyl)methylidene]amino}oxy)propanoic acid	COc1ccccc1C=N/OCCC(=O)O	HNYXMVDBRIIJGT-WQLSENKSSA-N
8BD	B	C11 H13 N O4	223.23	3-({[(1Z)-(2-methoxyphenyl)methylidene]amino}oxy)propanoic acid	COc1ccccc1C=N/OCCC(=O)O	HNYXMVDBRIIJGT-WQLSENKSSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Chemoselective small molecules that covalently modify one lysine in a non-enzyme protein in plasma; small molecule kinetic stabilizer

They report a family of designed stilbenes that selectively and covalently modify the prominent plasma protein transthyretin. They react chemoselectively with only one of eight lysine e-amino groups within transthyretin. Covalent transthyretin kinetic stabilizers exhibit superior amyloid inhibition potency compared to their noncovalent counterparts, and they prevent cytotoxicity associated with amyloidogenesis.

Literature

PMID:	20081815
Author(s):	Choi, S., Connelly, S., Reixach, N., Wilson, I.A., Kelly, J.W.
Reference:	Nat Chem Biol. 2010 Feb;6(2):133-9.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3HJ0
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.34
R free:	0.182

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
A93	A	C23 H19 F O3	362.39	4-fluorophenyl 3-[(E)-2-(4-hydroxy-3,5-dimethylphenyl)ethenyl]benzoate	Cc1cc(cc(c1O)C)C=Cc2cccc(c2)C(=O)Oc3ccc(cc3)F	YDSMVVNYVJZDET-VOTSOKGWSA-N
CSD	A	C3 H7 N O4 S	153.16	3-SULFINOALANINE	C([C@@H](C(=O)O)N)[S@@](=O)O	ADVPTQAUNPRNPO-REOHCLBHSA-N
A93	B	C23 H19 F O3	362.39	4-fluorophenyl 3-[(E)-2-(4-hydroxy-3,5-dimethylphenyl)ethenyl]benzoate	Cc1cc(cc(c1O)C)C=Cc2cccc(c2)C(=O)Oc3ccc(cc3)F	YDSMVVNYVJZDET-VOTSOKGWSA-N
CSD	B	C3 H7 N O4 S	153.16	3-SULFINOALANINE	C([C@@H](C(=O)O)N)[S@@](=O)O	ADVPTQAUNPRNPO-REOHCLBHSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

T

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

T

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Crystal structure of human transthyretin variant A25T

Crystal structure of amyloidogenic human transthyretin variant A25T

Literature

PMID:
Author(s):	Palmieri, L.C., Freire, J.B.B., Palhano, F.L., Azevedo, E.P.C., Foguel, D., Lima, L.M.T.R.
Reference:

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3I9A
Amyloid Category:	Amyloid
Type:	Protein
Global Stoichiometry:	Monomer - A
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.65
R free:	0.22699999

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
PGE	A	C6 H14 O4	150.17	TRIETHYLENE GLYCOL	C(COCCOCCO)O	ZIBGPFATKBEMQZ-UHFFFAOYSA-N
PGE	B	C6 H14 O4	150.17	TRIETHYLENE GLYCOL	C(COCCOCCO)O	ZIBGPFATKBEMQZ-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

T

I

N

V

A

V

H

V

F

R

25

26

K

A

D

T

W

E

P

F

A

S

G

K

T

S

E

S

G

E

L

H

G

L

T

50

51

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

K

S

Y

W

K

A

L

G

I

75

76

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

G

P

R

Y

T

I

A

100

101

L

S

P

Y

S

Y

S

T

A

V

T

N

P

116

Chain 2

1

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

T

I

N

V

A

V

H

V

F

R

25

26

K

A

D

T

W

E

P

F

A

S

G

K

T

S

E

S

G

E

L

H

G

L

T

50

51

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

K

S

Y

W

K

A

L

G

I

75

76

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

G

P

R

Y

T

I

A

100

101

L

S

P

Y

S

Y

S

T

A

V

T

N

P

116

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Crystal structure of human transthyretin variant A25T

Crystal structure of amyloidogenic human transthyretin variant A25T

Literature

PMID:
Author(s):	Palmieri, L.C., Freire, J.B.B., Palhano, F.L., Azevedo, E.P.C., Foguel, D., Lima, L.M.T.R.
Reference:

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	116
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3I9I
Amyloid Category:	Amyloid
Type:	Protein
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	hormone-binding protein
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.8
R free:	0.237

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
PGE	A	C6 H14 O4	150.17	TRIETHYLENE GLYCOL	C(COCCOCCO)O	ZIBGPFATKBEMQZ-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Transthyretin in complex with (E)-2,6-dibromo-4-(2,6-dichlorostyryl)phenol

They develop potent and selective TTR kinetic stabilizers that rescue cells from the cytotoxic effects of TTR amyloidogenesis using stilbene and dihydrostilbene analogues. Six analogues were definitively categorized as kinetic stabilizers by evaluating dissociation time-courses.

Literature

PMID:	20043671
Author(s):	Choi, S., Reixach, N., Connelly, S., Johnson, S.M., Wilson, I.A., Kelly, J.W.
Reference:	J Am Chem Soc. 2010 Feb 3;132(4):1359-70.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3IMR
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.7
R free:	0.217

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
IW1	A	C14 H8 Br2 Cl2 O	422.93	2,6-dibromo-4-[(E)-2-(2,6-dichlorophenyl)ethenyl]phenol	c1cc(c(c(c1)Cl)/C=C/c2cc(c(c(c2)Br)O)Br)Cl	RLPYELPZSFVXBH-SNAWJCMRSA-N
IW1	B	C14 H8 Br2 Cl2 O	422.93	2,6-dibromo-4-[(E)-2-(2,6-dichlorophenyl)ethenyl]phenol	c1cc(c(c(c1)Cl)/C=C/c2cc(c(c(c2)Br)O)Br)Cl	RLPYELPZSFVXBH-SNAWJCMRSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Transthyretin in complex with 2,6-dibromo-4-(2,6-dichlorophenethyl)phenol

They develop potent and selective TTR kinetic stabilizers that rescue cells from the cytotoxic effects of TTR amyloidogenesis using stilbene and dihydrostilbene analogues. Six analogues were definitively categorized as kinetic stabilizers by evaluating dissociation time-courses.

Literature

PMID:	20043671
Author(s):	Choi, S., Reixach, N., Connelly, S., Johnson, S.M., Wilson, I.A., Kelly, J.W.
Reference:	J Am Chem Soc. 2010 Feb 3;132(4):1359-70.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3IMS
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.4
R free:	0.19699999

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
IW2	A	C14 H10 Br2 Cl2 O	424.94	2,6-dibromo-4-[2-(2,6-dichlorophenyl)ethyl]phenol	c1cc(c(c(c1)Cl)CCc2cc(c(c(c2)Br)O)Br)Cl	ZTXSVCNYFKOGBX-UHFFFAOYSA-N
IW2	B	C14 H10 Br2 Cl2 O	424.94	2,6-dibromo-4-[2-(2,6-dichlorophenyl)ethyl]phenol	c1cc(c(c(c1)Cl)CCc2cc(c(c(c2)Br)O)Br)Cl	ZTXSVCNYFKOGBX-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Transthyretin in complex with (E)-4-(4-aminostyryl)-2,6-dibromophenol

They develop potent and selective TTR kinetic stabilizers that rescue cells from the cytotoxic effects of TTR amyloidogenesis using stilbene and dihydrostilbene analogues. Six analogues were definitively categorized as kinetic stabilizers by evaluating dissociation time-courses.

Literature

PMID:	20043671
Author(s):	Choi, S., Reixach, N., Connelly, S., Johnson, S.M., Wilson, I.A., Kelly, J.W.
Reference:	J Am Chem Soc. 2010 Feb 3;132(4):1359-70.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3IMT
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.4
R free:	0.19

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
IW3	A	C14 H11 Br2 N O	369.05	4-[(E)-2-(4-aminophenyl)ethenyl]-2,6-dibromophenol	c1cc(ccc1/C=C/c2cc(c(c(c2)Br)O)Br)N	AZVOHBNUGLEXNG-OWOJBTEDSA-N
IW3	B	C14 H11 Br2 N O	369.05	4-[(E)-2-(4-aminophenyl)ethenyl]-2,6-dibromophenol	c1cc(ccc1/C=C/c2cc(c(c(c2)Br)O)Br)N	AZVOHBNUGLEXNG-OWOJBTEDSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Transthyretin in complex with (E)-4-(3-aminostyryl)-2,6-dibromoaniline

They develop potent and selective TTR kinetic stabilizers that rescue cells from the cytotoxic effects of TTR amyloidogenesis using stilbene and dihydrostilbene analogues. Six analogues were definitively categorized as kinetic stabilizers by evaluating dissociation time-courses.

Literature

PMID:	20043671
Author(s):	Choi, S., Reixach, N., Connelly, S., Johnson, S.M., Wilson, I.A., Kelly, J.W.
Reference:	J Am Chem Soc. 2010 Feb 3;132(4):1359-70.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3IMU
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.4
R free:	0.191

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
IW4	A	C14 H12 Br2 N2	368.07	4-[(E)-2-(3-aminophenyl)ethenyl]-2,6-dibromoaniline	c1cc(cc(c1)N)/C=C/c2cc(c(c(c2)Br)N)Br	KYCYQIDURIMUDR-SNAWJCMRSA-N
IW4	B	C14 H12 Br2 N2	368.07	4-[(E)-2-(3-aminophenyl)ethenyl]-2,6-dibromoaniline	c1cc(cc(c1)N)/C=C/c2cc(c(c(c2)Br)N)Br	KYCYQIDURIMUDR-SNAWJCMRSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Transthyretin in complex with (E)-4-(4-aminostyryl)-2,6-dibromoaniline

They develop potent and selective TTR kinetic stabilizers that rescue cells from the cytotoxic effects of TTR amyloidogenesis using stilbene and dihydrostilbene analogues. Six analogues were definitively categorized as kinetic stabilizers by evaluating dissociation time-courses.

Literature

PMID:	20043671
Author(s):	Choi, S., Reixach, N., Connelly, S., Johnson, S.M., Wilson, I.A., Kelly, J.W.
Reference:	J Am Chem Soc. 2010 Feb 3;132(4):1359-70.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3IMV
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.47
R free:	0.201

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
IW5	A	C14 H12 Br2 N2	368.07	4-[(E)-2-(4-aminophenyl)ethenyl]-2,6-dibromoaniline	c1cc(ccc1/C=C/c2cc(c(c(c2)Br)N)Br)N	JADLJYGSTKXGCQ-OWOJBTEDSA-N
IW5	B	C14 H12 Br2 N2	368.07	4-[(E)-2-(4-aminophenyl)ethenyl]-2,6-dibromoaniline	c1cc(ccc1/C=C/c2cc(c(c(c2)Br)N)Br)N	JADLJYGSTKXGCQ-OWOJBTEDSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Transthyretin in complex with (E)-2,6-dibromo-4-(2,6-dimethoxystyryl)aniline

They develop potent and selective TTR kinetic stabilizers that rescue cells from the cytotoxic effects of TTR amyloidogenesis using stilbene and dihydrostilbene analogues. Six analogues were definitively categorized as kinetic stabilizers by evaluating dissociation time-courses.

Literature

PMID:	20043671
Author(s):	Choi, S., Reixach, N., Connelly, S., Johnson, S.M., Wilson, I.A., Kelly, J.W.
Reference:	J Am Chem Soc. 2010 Feb 3;132(4):1359-70.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3IMW
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.31
R free:	0.196

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
IW6	A	C16 H15 Br2 N O2	413.1	2,6-dibromo-4-[(E)-2-(2,6-dimethoxyphenyl)ethenyl]aniline	COc1cccc(c1/C=C/c2cc(c(c(c2)Br)N)Br)OC	HGWBUXCGPMRHAS-VOTSOKGWSA-N
IW6	B	C16 H15 Br2 N O2	413.1	2,6-dibromo-4-[(E)-2-(2,6-dimethoxyphenyl)ethenyl]aniline	COc1cccc(c1/C=C/c2cc(c(c(c2)Br)N)Br)OC	HGWBUXCGPMRHAS-VOTSOKGWSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Human Transthyretin (TTR) complexed with a palindromic bivalent amyloid inhibitor (11 carbon linker).

They have designed ligands that are rapidly bound by native wild-type TTR in whole serum and even more avidly by amyloidogenic TTR variants. X-ray crystallographic analysis shows simultaneous occupation of both T4 binding sites in each tetrameric TTR molecule by the pair of ligand head groups. Ligand binding by native TTR was irreversible under physiological conditions, and it stabilized the tetrameric assembly and inhibited amyloidogenic aggregation more potently than other known ligands. These superstabilizers are orally bioavailable and exhibit low inhibitory activity against cyclooxygenase (COX).

Literature

PMID:	21059958
Author(s):	Kolstoe, S.E., Mangione, P.P., Bellotti, V., Taylor, G.W., Tennent, G.A., Deroo, S., Morrison, A.J., Cobb, A.J., Coyne, A., McCammon, M.G., Warner, T.D., Mitchell, J., Gill, R., Smith, M.D., Ley, S.V., Robinson, C.V., Wood, S.P., Pepys, M.B.
Reference:	Proc Natl Acad Sci U S A. 2010 Nov 23;107(47):20483-8.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3IPB
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.9
R free:	0.22899999

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
JZD	A	C37 H38 Cl4 N2 O6	748.52	2,2'-{undecane-1,11-diylbis[oxy(3,5-dichlorobenzene-4,1-diyl)imino]}dibenzoic acid	c1ccc(c(c1)C(=O)O)Nc2cc(c(c(c2)Cl)OCCCCCCCCCCCOc3c(cc(cc3Cl)Nc4ccccc4C(=O)O)Cl)Cl	GZMGFINVSIBSLS-UHFFFAOYSA-N
JZD	B	C37 H38 Cl4 N2 O6	748.52	2,2'-{undecane-1,11-diylbis[oxy(3,5-dichlorobenzene-4,1-diyl)imino]}dibenzoic acid	c1ccc(c(c1)C(=O)O)Nc2cc(c(c(c2)Cl)OCCCCCCCCCCCOc3c(cc(cc3Cl)Nc4ccccc4C(=O)O)Cl)Cl	GZMGFINVSIBSLS-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Human Transthyretin (TTR) complexed with a palindromic bivalent amyloid inhibitor (7 carbon linker).

They have designed ligands that are rapidly bound by native wild-type TTR in whole serum and even more avidly by amyloidogenic TTR variants. X-ray crystallographic analysis shows simultaneous occupation of both T4 binding sites in each tetrameric TTR molecule by the pair of ligand head groups. Ligand binding by native TTR was irreversible under physiological conditions, and it stabilized the tetrameric assembly and inhibited amyloidogenic aggregation more potently than other known ligands. These superstabilizers are orally bioavailable and exhibit low inhibitory activity against cyclooxygenase (COX).

Literature

PMID:	21059958
Author(s):	Kolstoe, S.E., Mangione, P.P., Bellotti, V., Taylor, G.W., Tennent, G.A., Deroo, S., Morrison, A.J., Cobb, A.J., Coyne, A., McCammon, M.G., Warner, T.D., Mitchell, J., Gill, R., Smith, M.D., Ley, S.V., Robinson, C.V., Wood, S.P., Pepys, M.B.
Reference:	Proc Natl Acad Sci U S A. 2010 Nov 23;107(47):20483-8.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3IPE
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.4
R free:	0.196

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
JZE	B	C33 H30 Cl4 N2 O6	692.41	2,2'-{heptane-1,7-diylbis[oxy(3,5-dichlorobenzene-4,1-diyl)imino]}dibenzoic acid	c1ccc(c(c1)C(=O)O)Nc2cc(c(c(c2)Cl)OCCCCCCCOc3c(cc(cc3Cl)Nc4ccccc4C(=O)O)Cl)Cl	PVJQFPTYHVNSAO-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

N

L

Y

Q

F

K

N

M

I

Q

C

T

V

P

S

R

S

W

A

D

F

A

D

Y

G

25

26

C

Y

C

G

K

G

S

G

T

P

V

D

L

D

R

C

Q

T

H

D

N

C

50

51

Y

N

E

A

E

N

I

S

G

C

R

P

Y

F

K

T

Y

S

Y

E

C

T

Q

G

T

75

76

L

T

C

K

G

D

N

A

C

A

S

V

C

D

C

D

R

L

A

I

C

F

100

101

A

G

A

P

Y

N

D

A

N

Y

N

I

D

L

K

A

R

C

N

119

Chain 2

1

D

A

E

F

R

H

D

S

8

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Phospholipase A2 Prevents the Aggregation of Amyloid Beta Peptides: Crystal Structure of the Complex of Phospholipase A2 with Octapeptide Fragment of Amyloid Beta Peptide, Asp-Ala-Glu-Phe-Arg-His-Asp-Ser at 2 A Resolution

Phospholipase A2 Prevents the Aggregation of Amyloid Beta Peptides

Literature

PMID:
Author(s):	Mirza, Z., Vikram, G., Singh, N., Sinha, M., Bhushan, A., Sharma, S., Srinivasan, A., Kaur, P., Singh, T.P.
Reference:

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Amyloid-beta
Alternative Name:	Phosphatidylcholine 2-acylhydrolase & ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II
Gene Name:	APP, A4, AD1
Sequence Length:	119 , 8
Species:
Mutation(s):	No
E.C. Number:	3.1.1.4
UniProt ID:
Keyword(s):

Structure Information

PDB ID:	3JQ5
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Monomer - A
PDB Classification:	HYDROLASE
Method:	X-RAY DIFFRACTION
Resolution (Å):	2.03
R free:	0.221

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
CA	A	Ca 2	40.08	CALCIUM ION	[Ca+2]	BHPQYMZQTOCNFJ-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

M

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

M

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

V30M mutant human transthyretin (TTR) complexed with genistein (V30M:GEN) pH 7.5

Isoflavone genistein (GEN) potently inhibits TTR amyloid fibril formation and is therefore a promising candidate for TTR amyloidosis treatment. Genistein elicited considerable increases in both mutant and TTRwt stability. The binding mechanisms of genistein to the TTRwt and to V30M are different and are dependent on apoTTR structure conformations.

Literature

PMID:	20211733
Author(s):	Trivella, D.B., Bleicher, L., Palmieri, L.C., Wiggers, H.J., Montanari, C.A., Kelly, J.W., Lima, L.M., Foguel, D., Polikarpov, I.
Reference:	J Struct Biol. 2010 Jun;170(3):522-31.

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	V30M
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3KGT
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	TRANSPORT PROTEIN
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.95
R free:	0.24100000

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
GEN	A	C15 H10 O5	270.24	GENISTEIN	c1cc(ccc1C2=COc3cc(cc(c3C2=O)O)O)O	TZBJGXHYKVUXJN-UHFFFAOYSA-N
GEN	B	C15 H10 O5	270.24	GENISTEIN	c1cc(ccc1C2=COc3cc(cc(c3C2=O)O)O)O	TZBJGXHYKVUXJN-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Wild type human transthyretin (TTR) complexed with genistein (TTRwt:GEN) pH 7.5

Isoflavone genistein (GEN) potently inhibits TTR amyloid fibril formation and is therefore a promising candidate for TTR amyloidosis treatment. Genistein elicited considerable increases in both mutant and TTRwt stability. The binding mechanisms of genistein to the TTRwt and to V30M are different and are dependent on apoTTR structure conformations.

Literature

PMID:	20211733
Author(s):	Trivella, D.B., Bleicher, L., Palmieri, L.C., Wiggers, H.J., Montanari, C.A., Kelly, J.W., Lima, L.M., Foguel, D., Polikarpov, I.
Reference:	J Struct Biol. 2010 Jun;170(3):522-31.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3KGU
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	TRANSPORT PROTEIN
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.85
R free:	0.23399999

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
GEN	A	C15 H10 O5	270.24	GENISTEIN	c1cc(ccc1C2=COc3cc(cc(c3C2=O)O)O)O	TZBJGXHYKVUXJN-UHFFFAOYSA-N
GEN	B	C15 H10 O5	270.24	GENISTEIN	c1cc(ccc1C2=COc3cc(cc(c3C2=O)O)O)O	TZBJGXHYKVUXJN-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

D

Y

K

D

E

V

Q

L

V

E

S

G

L

V

Q

P

G

S

L

R

L

S

25

26

C

T

A

S

G

Y

T

F

S

H

R

Y

H

R

W

F

R

Q

A

P

G

K

E

R

E

50

51

I

V

A

V

I

S

Q

S

G

M

R

T

Y

A

D

S

V

K

G

R

F

T

I

S

75

76

R

D

N

A

K

N

T

V

Y

L

Q

M

N

S

L

K

P

E

D

T

A

M

Y

C

100

101

A

G

T

R

K

N

V

W

T

R

Q

H

P

F

D

Y

W

G

Q

G

T

Q

V

T

125

126

V

S

A

S

G

A

D

H

139

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Crystal structure of the fibril-specific B10 antibody fragment; B10 crystal structure and model of fibril binding (PDB id: 2ONV)

B10 antibody fragment presents poly-amyloid specific binding and interacts with fibrillar structures consisting of different polypeptide chains (selectively binds to Alzheimer's ABeta(1-40) amyloid fibrils). Fibril recognition depends on positively charged residues within the B10 antigen binding site. Mutation of these basic residues into alanine potently impairs fibril binding, and reduced B10-fibril interactions are also observed when the fibril carboxyl groups are covalently masked by a chemical modification approach.

Literature

PMID:	21059358
Author(s):	Haupt, C., Morgado, I., Kumar, S.T., Parthier, C., Bereza, M., Hortschansky, P., Stubbs, M.T., Horn, U., Fandrich, M.
Reference:	J Mol Biol. 2011 Jan 14;405(2):341-8.

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	B10 Antibody Fragment
Alternative Name:
Gene Name:
Sequence Length:	139
Species:	Camelidae
Mutation(s):	No
E.C. Number:
UniProt ID:
Keyword(s):	Immunoglobulin heavy chain antibody variable domain B10

Structure Information

PDB ID:	3LN9
Amyloid Category:	Amyloid
Type:	Fibril complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	IMMUNE SYSTEM
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.8
R free:	0.233

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
FLC	A	C6 H5 O7 -3	189.1	CITRATE ANION	C(C(=O)[O-])C(CC(=O)[O-])(C(=O)[O-])O	KRKNYBCHXYNGOX-UHFFFAOYSA-K
GOL	A	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
SO4	A	O4 S -2	96.06	SULFATE ION	[O-]S(=O)(=O)[O-]	QAOWNCQODCNURD-UHFFFAOYSA-L

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

M

I

Q

R

T

P

K

I

Q

V

Y

S

R

H

P

A

E

N

G

K

S

N

F

L

N

25

26

C

Y

V

S

G

F

H

P

S

D

I

E

V

D

L

K

N

G

E

R

I

E

K

V

50

51

E

H

S

D

L

S

F

S

K

D

W

S

F

Y

L

Y

T

E

F

T

P

T

E

75

76

K

D

E

Y

A

C

R

V

N

H

V

T

L

S

Q

P

K

I

V

K

W

D

R

D

M

100

Chain 2

1

M

I

Q

R

T

P

K

I

Q

V

Y

S

R

H

P

A

E

N

G

K

S

N

F

L

N

25

26

C

Y

V

S

G

F

H

P

S

D

I

E

V

D

L

K

N

G

E

R

I

E

K

V

50

51

E

H

S

D

L

S

F

S

K

D

W

S

F

Y

L

Y

T

E

F

T

P

T

E

75

76

K

D

E

Y

A

C

R

V

N

H

V

T

L

S

Q

P

K

I

V

K

W

D

R

D

M

100

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Crystal structure of Beta 2 Microglobulin domain-swapped dimer

They show that b2m can oligomerize and fibrillize via three-dimensional domain swapping. Isolating a covalently bound, domain-swapped dimer from Beta?m oligomers on the pathway to fibrils. They were able to determine its crystal structure.

Literature

PMID:	21131979
Author(s):	Liu, C., Sawaya, M.R., Eisenberg, D.
Reference:	Nat Struct Mol Biol. 2011 Jan;18(1):49-55.

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Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Beta-2-microglobulin
Alternative Name:
Gene Name:	B2M, CDABP0092, HDCMA22P
Sequence Length:	100
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P61769
Keyword(s):	Beta-2-microglobulin

Structure Information

PDB ID:	3LOW
Amyloid Category:	Amyloid
Type:	Protein
Global Stoichiometry:	Homo 2-mer - A2
PDB Classification:	PROTEIN FIBRIL
Method:	X-RAY DIFFRACTION
Resolution (Å):	2.3
R free:	0.266

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
GOL	A	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
GOL	B	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Chain 2

1

G

P

T

G

T

G

E

S

K

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

25

26

I

N

V

A

V

H

V

F

R

K

A

D

T

W

E

P

F

A

S

G

K

T

S

50

51

E

S

G

E

L

H

G

L

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

75

76

K

S

Y

W

K

A

L

G

I

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

100

101

G

P

R

Y

T

I

A

L

S

P

Y

S

Y

S

T

A

V

T

N

P

125

126

K

E

127

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Human Transthyretin (TTR) complexed with 2-((3,5-dichloro-4-hydroxyphenyl)amino)benzoic acid

They have designed ligands that are rapidly bound by native wild-type TTR in whole serum and even more avidly by amyloidogenic TTR variants. X-ray crystallographic analysis shows simultaneous occupation of both T4 binding sites in each tetrameric TTR molecule by the pair of ligand head groups. Ligand binding by native TTR was irreversible under physiological conditions, and it stabilized the tetrameric assembly and inhibited amyloidogenic aggregation more potently than other known ligands. These superstabilizers are orally bioavailable and exhibit low inhibitory activity against cyclooxygenase (COX).

Literature

PMID:	21059958
Author(s):	Kolstoe, S.E., Mangione, P.P., Bellotti, V., Taylor, G.W., Tennent, G.A., Deroo, S., Morrison, A.J., Cobb, A.J., Coyne, A., McCammon, M.G., Warner, T.D., Mitchell, J., Gill, R., Smith, M.D., Ley, S.V., Robinson, C.V., Wood, S.P., Pepys, M.B.
Reference:	Proc Natl Acad Sci U S A. 2010 Nov 23;107(47):20483-8.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	127
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3M1O
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	HORMONE
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.2
R free:	0.171

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
CJZ	A	C13 H9 Cl2 N O3	298.12	2-[(3,5-dichloro-4-hydroxyphenyl)amino]benzoic acid	c1ccc(c(c1)C(=O)O)Nc2cc(c(c(c2)Cl)O)Cl	AKTRZQGZDAYEOG-UHFFFAOYSA-N
CJZ	B	C13 H9 Cl2 N O3	298.12	2-[(3,5-dichloro-4-hydroxyphenyl)amino]benzoic acid	c1ccc(c(c1)C(=O)O)Nc2cc(c(c(c2)Cl)O)Cl	AKTRZQGZDAYEOG-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

M

I

Q

R

T

P

K

I

Q

V

Y

S

R

H

P

A

E

N

G

K

S

N

F

L

N

25

26

C

Y

V

S

G

F

H

P

S

D

I

E

V

D

L

K

N

G

E

R

I

E

K

V

50

51

E

H

S

P

L

S

F

S

K

D

W

S

F

Y

L

Y

T

E

F

T

P

T

E

75

76

K

D

E

Y

A

C

R

V

N

H

V

T

L

S

Q

P

K

I

V

K

W

D

R

D

M

100

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

D-strand perturbation and amyloid propensity in beta-2 microglobulin

The mutation Asp53Pro was engineered in Beta2m, aiming to impair the formation of a regular/straight D-strand. The results reported in the present study highlight the conformational plasticity of the edge D-strand, and show that even perturbing the D-strand structure through a Pro residue has only marginal effects on protecting Beta2m from amyloid aggregation in vitro.

Literature

PMID:	21569201
Author(s):	Azinas, S., Colombo, M., Barbiroli, A., Santambrogio, C., Giorgetti, S., Raimondi, S., Bonomi, F., Grandori, R., Bellotti, V., Ricagno, S., Bolognesi, M.
Reference:	FEBS J. 2011 Jul;278(13):2349-58.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Beta-2-microglobulin
Alternative Name:
Gene Name:	B2M, CDABP0092, HDCMA22P
Sequence Length:	100
Species:	Homo sapiens
Mutation(s):	D53P
E.C. Number:
UniProt ID:	P61769
Keyword(s):	Beta-2-microglobulin

Structure Information

PDB ID:	3NA4
Amyloid Category:	Amyloid
Type:	Protein
Global Stoichiometry:	Monomer - A
PDB Classification:	IMMUNE SYSTEM
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.9
R free:	0.26899999

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
CSO	A	C3 H7 N O3 S	137.16	S-HYDROXYCYSTEINE	C([C@@H](C(=O)O)N)SO	FXIRVRPOOYSARH-REOHCLBHSA-N
PE4	A	C16 H34 O8	354.44	2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL	CCOCCOCCOCCOCCOCCOCCOCCO	PJWQOENWHPEPKI-UHFFFAOYSA-N

Structure

Press 'p' to pause
View interactive contact network
Protein Contacts Atlas

Sequence & Sec. Str.

Chain 1

1

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

I

N

V

A

V

H

V

F

R

25

26

K

A

D

T

W

E

P

F

A

S

G

K

T

S

E

S

G

E

L

H

G

L

T

50

51

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

K

S

Y

W

K

A

L

G

I

75

76

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

G

P

R

Y

T

I

A

100

101

L

S

P

Y

S

Y

S

T

A

V

T

N

P

116

Chain 2

1

C

P

L

M

V

K

V

L

D

A

V

R

G

S

P

A

I

N

V

A

V

H

V

F

R

25

26

K

A

D

T

W

E

P

F

A

S

G

K

T

S

E

S

G

E

L

H

G

L

T

50

51

T

E

F

V

E

G

I

Y

K

V

E

I

D

T

K

S

Y

W

K

A

L

G

I

75

76

S

P

F

H

E

H

A

E

V

F

T

A

N

D

S

G

P

R

Y

T

I

A

100

101

L

S

P

Y

S

Y

S

T

A

V

T

N

P

116

Helix: Magenta; Strand: Yellow; Coil & Turn: White.

Charged residues and Proline are highlighed in blue.

Description

Wild type human transthyretin (TTR) complexed with GC-1 (TTRwt:GC-1)

They characterized the interactions of the synthetic triiodo L-thyronine analogs and thyroid hormone nuclear receptor TR-Beta-selective agonists GC-1 and GC-24 with the wild type and V30M variant of human transthyretin (TTR). The data indicate that both GC-1 and GC-24 bind to TTR in a non-cooperative manner and are good inhibitors of TTR aggregation

Literature

PMID:	20937391
Author(s):	Trivella, D.B., Sairre, M.I., Foguel, D., Lima, L.M., Polikarpov, I.
Reference:	J Struct Biol. 2011 Feb;173(2):323-32.

Download

Entry:	CSV JSON
Structure:	PDB CIF FASTA
Contact Network:	CSV JSON

Protein Information

Protein Name:	Transthyretin
Alternative Name:	ATTR, Prealbumin, TBPA
Gene Name:	TTR, PALB
Sequence Length:	116
Species:	Homo sapiens
Mutation(s):	No
E.C. Number:
UniProt ID:	P02766
Keyword(s):	Transthyretin

Structure Information

PDB ID:	3NEE
Amyloid Category:	Non-amyloid
Type:	Inhibitor complex
Global Stoichiometry:	Homo 4-mer - A4
PDB Classification:	TRANSPORT PROTEIN
Method:	X-RAY DIFFRACTION
Resolution (Å):	1.55
R free:	0.217

Ligand Information

Ligand ID	Chain ID	Ligand Formula	Ligand MW	Ligand Name	Ligand SMILES	InChI Key
B72	A	C20 H24 O4	328.4	{4-[4-hydroxy-3-(1-methylethyl)benzyl]-3,5-dimethylphenoxy}acetic acid	Cc1cc(cc(c1Cc2ccc(c(c2)C(C)C)O)C)OCC(=O)O	QNAZTOHXCZPOSA-UHFFFAOYSA-N
GOL	A	C3 H8 O3	92.09	GLYCEROL	C(C(CO)O)O	PEDCQBHIVMGVHV-UHFFFAOYSA-N
B72	B	C20 H24 O4	328.4	{4-[4-hydroxy-3-(1-methylethyl)benzyl]-3,5-dimethylphenoxy}acetic acid	Cc1cc(cc(c1Cc2ccc(c(c2)C(C)C)O)C)OCC(=O)O	QNAZTOHXCZPOSA-UHFFFAOYSA-N

Structure database of aggregation related proteins and peptides

Displaying 241 to 270 records out of 565 records fetched.