Structure of PDB 1bgq Chain A Binding Site BS01

Receptor Information
>1bgq Chain A (length=214) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSL
SDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSG
TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWES
NAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEF
VAYPIQLVVTKEVE
Ligand information
Ligand IDRDC
InChIInChI=1S/C18H17ClO6/c1-9-6-15-14(25-15)5-3-2-4-10(20)7-11-16(18(23)24-9)12(21)8-13(22)17(11)19/h2-5,8-9,14-15,21-22H,6-7H2,1H3/b4-2+,5-3-/t9-,14-,15-/m1/s1
InChIKeyWYZWZEOGROVVHK-GTMNPGAYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC1CC2C(O2)C=CC=CC(=O)Cc3c(c(cc(c3Cl)O)O)C(=O)O1
OpenEye OEToolkits 1.5.0C[C@@H]1C[C@@H]2[C@H](O2)\C=C/C=C/C(=O)Cc3c(c(cc(c3Cl)O)O)C(=O)O1
CACTVS 3.341C[C@@H]1C[C@H]2O[C@@H]2\C=C/C=C/C(=O)Cc3c(Cl)c(O)cc(O)c3C(=O)O1
ACDLabs 10.04O=C2C=CC=CC3OC3CC(OC(=O)c1c(O)cc(O)c(Cl)c1C2)C
CACTVS 3.341C[CH]1C[CH]2O[CH]2C=CC=CC(=O)Cc3c(Cl)c(O)cc(O)c3C(=O)O1
FormulaC18 H17 Cl O6
NameRADICICOL;
MONORDEN
ChEMBLCHEMBL414883
DrugBankDB03758
ZINCZINC000013521629
PDB chain1bgq Chain A Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1bgq Structural basis for inhibition of the Hsp90 molecular chaperone by the antitumor antibiotics radicicol and geldanamycin.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		N37 D40 K44 D79 M84 F124 L173
Binding residue
(residue number reindexed from 1)		N37 D40 K44 D79 M84 F124 L173
Annotation score1
Binding affinityMOAD: Kd=2.7nM
PDBbind-CN: -logKd/Ki=8.57,Kd=2.7nM
BindingDB: IC50=2e+2nM
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1bgq, PDBe:1bgq, PDBj:1bgq
PDBsum1bgq
PubMed9925731
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

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