{"remarks": "CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN IN COMPLEX WITH O-TRIFLUOROMETHYLPHENYL ANTHRANILIC ACID", "ligand_id": "OFL", "secondary_structure": "GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEQFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEESTTSCCEEEEEEEEETTEEEEEEEEEC&GPTGTGESKCPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEQFVEGIYKVEIDTKSYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN#CCCCCCCCCCCEEEEEEETTTTEECTTCEEEEEEECTTSCEEEEEEEECCTTSEECCSCCTTTCCSEEEEEEECHHHHHHHTTCCCSEEEEEEEEEECCSSSCCEEEEEEEETTEEEEEEEECC", "mutation_s_field": "No", "keyword": "TRANSTHYRETIN", "ligstr": "OFL:A:C14 H10 F3 N O2:281.23:O-TRIFLUOROMETHYLPHENYL ANTHRANILIC ACID:c1ccc(c(c1)C(=O)O)Nc2ccccc2C(F)(F)F:InChI=1S/C14H10F3NO2/c15-14(16,17)10-6-2-4-8-12(10)18-11-7-3-1-5-9(11)13(19)20/h1-8,18H,(H,19,20):ONKHJNFXJDEMNQ-UHFFFAOYSA-N", "alternative_name": "ATTR, Prealbumin, TBPA", "species": "Homo sapiens", "r_value_free": "0.2", "pdb_id": "1DVZ", "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": "c1ccc(c(c1)C(=O)O)Nc2ccccc2C(F)(F)F", "author": "Klabunde, T., Petrassi, H.M., Oza, V.B., Raman, P., Kelly, J.W., Sacchettini, J.C.", "description": "The crystal structure of the TTR\u00e2\u20ac\u201coFLU complex shows that oFLU binds deep in the two funnel-shaped hormone-binding cavities located at the dimer\u00e2\u20ac\u201cdimer interface of TTR. The carboxylate-substituted phenyl ring is positioned near the entry of the binding channel. the trifluoromethyl-substituted phenyl ring of oFLU fits well into HBP-3 and HBP-3?. Both, the phenyl ring and the CF3 group, show favorable van der Waals packing with the side chains of Ala 108, Ala 109, Leu 110, Ser 117 and Thr 119 from two adjacent TTR subunits, thus contributing to the stabilization of the tetrameric structure of TTR. However, a slight rotation of the carboxylate-substituted phenyl ring of the inhibitor prohibits the carboxylate group of oFLU from forming a direct electrostatic interaction with the amino group of Lys 15, as observed for the TTR\u00e2\u20ac\u201cFLU structure. Instead, in the TTR\u00e2\u20ac\u201coFLU complex, a hydrogen bond between these groups was mediated via an ordered water molecule. ", "ligand_mw": "281.23", "entry": "S-0023", "ligand_name": "O-TRIFLUOROMETHYLPHENYL ANTHRANILIC ACID", "pdb_classification": "HORMONE/GROWTH FACTOR", "amyloid_non_amyloid": "Non-amyloid", "chain_id": "A", "inchi_key": "ONKHJNFXJDEMNQ-UHFFFAOYSA-N", "gene_names": "TTR, PALB", "method": "X-RAY DIFFRACTION", "length": "124", "inchi": "InChI=1S/C14H10F3NO2/c15-14(16,17)10-6-2-4-8-12(10)18-11-7-3-1-5-9(11)13(19)20/h1-8,18H,(H,19,20)", "type": "Inhibitor complex", "reference": "Nat Struct Biol. 2000 Apr;7(4):312-21", "ligand_formula": "C14 H10 F3 N O2"}