Structure of PDB 4i89 Chain A Binding Site BS01

Receptor Information
>4i89 Chain A (length=116) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
CPLMVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESGELHGLT
TEEEFVEGIYKVEIDTKSYWKALGSSPFHEHAEVVFTANDSGPRRYTIAA
LLSPYSYSTTAVVTNP
Ligand information
Ligand ID1FL
InChIInChI=1S/C13H8F2O3/c14-8-2-3-9(11(15)6-8)7-1-4-12(16)10(5-7)13(17)18/h1-6,16H,(H,17,18)
InChIKeyHUPFGZXOMWLGNK-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(=O)c1cc(ccc1O)c2ccc(F)cc2F
OpenEye OEToolkits 1.5.0c1cc(c(cc1c2ccc(cc2F)F)C(=O)O)O
ACDLabs 10.04O=C(O)c1cc(ccc1O)c2ccc(F)cc2F
FormulaC13 H8 F2 O3
Name5-(2,4-DIFLUOROPHENYL)-2-HYDROXY-BENZOIC ACID;
Diflunisal
ChEMBLCHEMBL898
DrugBankDB00861
ZINCZINC000000020243
PDB chain4i89 Chain A Residue 201 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4i89 Structural evidence for native state stabilization of a conformationally labile amyloidogenic transthyretin variant by fibrillogenesis inhibitors.
Resolution1.69 Å
Binding residue
(original residue number in PDB)		K15 L17 A108 L110 S117 T118 T119
Binding residue
(residue number reindexed from 1)		K6 L8 A99 L101 S108 T109 T110
Annotation score1
Binding affinityBindingDB: IC50=12000nM,Kd=407nM,EC50=5600nM
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005179 hormone activity
GO:0005515 protein binding
GO:0042802 identical protein binding
GO:0070324 thyroid hormone binding
Biological Process
GO:0006144 purine nucleobase metabolic process
GO:0007165 signal transduction
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005737 cytoplasm
GO:0035578 azurophil granule lumen
GO:0070062 extracellular exosome

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4i89, PDBe:4i89, PDBj:4i89
PDBsum4i89
PubMed23792159
UniProtP02766|TTHY_HUMAN Transthyretin (Gene Name=TTR)

[Back to BioLiP]