{"remarks": "CRYSTAL STRUCTURE OF TRANSTHYRETIN IN COMPLEX WITH N-(M-TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID", "ligand_id": "BPD", "secondary_structure": "GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEQFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHTTTCCCSEEEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEEC&GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEQFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHTTTCCCSEEEEEEEEEECCSSSCCEEEEEEEETTEEEEEEEECC", "mutation_s_field": "No", "keyword": "TRANSTHYRETIN", "ligstr": "BPD:A:C21 H12 F3 N O5:415.32:N-(M-TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID:c1cc(cc(c1)N2c3cccc(c3Oc4c2cccc4C(=O)O)C(=O)O)C(F)(F)F:InChI=1S/C21H12F3NO5/c22-21(23,24)11-4-1-5-12(10-11)25-15-8-2-6-13(19(26)27)17(15)30-18-14(20(28)29)7-3-9-16(18)25/h1-10H,(H,26,27)(H,28,29):NQOOJFXBGLOGTC-UHFFFAOYSA-N", "alternative_name": "ATTR, Prealbumin, TBPA", "species": "Homo sapiens", "r_value_free": "0.203", "pdb_id": "1DVY", "pmid": "10742177", "peptide_protein_sequence": "chain-ID A: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEQFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN; chain-ID B: GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEQFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN", "resolution": "1.9", "ec_number": "", "uniprot_ac": "P02766", "protein_name": "Transthyretin", "global_stoichiometry": "Homo 4-mer - A4 ", "ligand_smiles": "c1cc(cc(c1)N2c3cccc(c3Oc4c2cccc4C(=O)O)C(=O)O)C(F)(F)F", "author": "Klabunde, T., Petrassi, H.M., Oza, V.B., Raman, P., Kelly, J.W., Sacchettini, J.C.", "description": "N-phenyl phenoxazine-4,6-dicarboxylate was constructed computationally and modeled to completely fill the available inner cavity of the hormone binding sites. PHENOX stabilizes the native TTR tetramer thus inhibiting the formation of amyloid fibrils. The crystal structure of TTR in complex with PHENOX shows the N-phenyl-substituted phenoxazine bound in its low energy conformation, with the planes of the distal phenyl ring and the tricyclic ring system almost orthogonal to each other. Extensive van der Waals interactions with the protein are observed, including those with the side chains of Thr 106, Lys 15 and Leu 17 from two adjacent subunits. The trifluoromethyl group of PHENOX does not bind as deep in the halogen binding pocket as the corresponding substituent of flufenamic acid. . However, PHENOX binds deep enough to displace an ordered water molecule found in the HBP-3 of apo-TTR. ", "ligand_mw": "415.32", "entry": "S-0022", "ligand_name": "N-(M-TRIFLUOROMETHYLPHENYL) PHENOXAZINE-4,6-DICARBOXYLIC ACID", "pdb_classification": "HORMONE/GROWTH FACTOR", "amyloid_non_amyloid": "Non-amyloid", "chain_id": "A", "inchi_key": "NQOOJFXBGLOGTC-UHFFFAOYSA-N", "gene_names": "TTR, PALB", "method": "X-RAY DIFFRACTION", "length": "124", "inchi": "InChI=1S/C21H12F3NO5/c22-21(23,24)11-4-1-5-12(10-11)25-15-8-2-6-13(19(26)27)17(15)30-18-14(20(28)29)7-3-9-16(18)25/h1-10H,(H,26,27)(H,28,29)", "type": "Inhibitor complex", "reference": "Nat Struct Biol. 2000 Apr;7(4):312-21", "ligand_formula": "C21 H12 F3 N O5"}