Structure of PDB 2fxs Chain A Binding Site BS01

Receptor Information
>2fxs Chain A (length=213) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLS
DPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGT
KAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESN
AGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFV
AYPIQLVVTKEVE
Ligand information
Ligand IDRDA
InChIInChI=1S/C18H18ClNO8/c1-27-14-7-10(21)9(5-11(14)22)20-15(25)4-3-8-16(18(26)28-2)12(23)6-13(24)17(8)19/h5-7,21-24H,3-4H2,1-2H3,(H,20,25)
InChIKeyGUVWEHNRWHNDRF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341COC(=O)c1c(O)cc(O)c(Cl)c1CCC(=O)Nc2cc(O)c(OC)cc2O
OpenEye OEToolkits 1.5.0COc1cc(c(cc1O)NC(=O)CCc2c(c(cc(c2Cl)O)O)C(=O)OC)O
ACDLabs 10.04Clc1c(c(c(O)cc1O)C(=O)OC)CCC(=O)Nc2cc(O)c(OC)cc2O
FormulaC18 H18 Cl N O8
NameMETHYL 3-CHLORO-2-{3-[(2,5-DIHYDROXY-4-METHOXYPHENYL)AMINO]-3-OXOPROPYL}-4,6-DIHYDROXYBENZOATE
ChEMBL
DrugBankDB08464
ZINCZINC000024798681
PDB chain2fxs Chain A Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fxs Different poses for ligand and chaperone in inhibitor-bound Hsp90 and GRP94: implications for paralog-specific drug design.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		N37 A41 K44 D79 M84 N92 F124 T171 L173
Binding residue
(residue number reindexed from 1)		N36 A40 K43 D78 M83 N91 F123 T170 L172
Annotation score1
Binding affinityMOAD: Kd=0.87uM
PDBbind-CN: -logKd/Ki=6.06,Kd=0.87uM
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

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Molecular Function
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Biological Process
External links
PDB RCSB:2fxs, PDBe:2fxs, PDBj:2fxs
PDBsum2fxs
PubMed19361515
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

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