Structure of PDB 2yga Chain A Binding Site BS01

Receptor Information
>2yga 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
SDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAGLINLLGTIAKSG
TKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWES
NAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEF
VAYPIQLVVTKEVE
Ligand information
Ligand IDGDM
InChIInChI=1S/C29H40N2O9/c1-15-11-19-25(34)20(14-21(32)27(19)39-7)31-28(35)16(2)9-8-10-22(37-5)26(40-29(30)36)18(4)13-17(3)24(33)23(12-15)38-6/h8-10,13-15,17,22-24,26,33H,11-12H2,1-7H3,(H2,30,36)(H,31,35)/b10-8-,16-9+,18-13+/t15-,17+,22+,23+,24-,26+/m1/s1
InChIKeyQTQAWLPCGQOSGP-KSRBKZBZSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC1CC(C(C(C=C(C(C(C=CC=C(C(=O)NC2=CC(=O)C(=C(C1)C2=O)OC)C)OC)OC(=O)N)C)C)O)OC
ACDLabs 10.04O=C1C(OC)=C2C(=O)C(=C1)NC(=O)C(=CC=CC(OC)C(OC(=O)N)C(=CC(C)C(O)C(OC)CC(C)C2)C)C
OpenEye OEToolkits 1.5.0C[C@H]1C[C@@H]([C@@H]([C@H](\C=C(\[C@@H]([C@H](\C=C/C=C(/C(=O)NC2=CC(=O)C(=C(C1)C2=O)OC)\C)OC)OC(=O)N)/C)C)O)OC
CACTVS 3.341CO[C@H]1C[C@H](C)CC2=C(OC)C(=O)C=C(NC(=O)\C(=C\C=C/[C@H](OC)[C@@H](OC(N)=O)\C(=C\[C@H](C)[C@H]1O)C)C)C2=O
CACTVS 3.341CO[CH]1C[CH](C)CC2=C(OC)C(=O)C=C(NC(=O)C(=CC=C[CH](OC)[CH](OC(N)=O)C(=C[CH](C)[CH]1O)C)C)C2=O
FormulaC29 H40 N2 O9
NameGELDANAMYCIN
ChEMBLCHEMBL278315
DrugBankDB02424
ZINCZINC000100064834
PDB chain2yga Chain A Residue 1215 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2yga Features of the Streptomyces Hygroscopicus Htpg Reveal How Partial Geldanamycin Resistance Can Arise with Mutation to the ATP Binding Pocket of a Eukaryotic Hsp90.
Resolution2.37 Å
Binding residue
(original residue number in PDB)		N37 D40 K44 M84 L92 K98 G121 V122 F124
Binding residue
(residue number reindexed from 1)		N37 D40 K44 M84 L92 K98 G121 V122 F124
Annotation score1
Binding affinityMOAD: Kd=24.5uM
PDBbind-CN: -logKd/Ki=4.61,Kd=24.5uM
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:2yga, PDBe:2yga, PDBj:2yga
PDBsum2yga
PubMed21778327
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

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