Structure of PDB 2ygf Chain A Binding Site BS01

Receptor Information
>2ygf 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
DPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAEVINNIGTIAKSGT
KAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQMISKSNDDEQYIWESN
AGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFV
AYPIQLVVTKEVE
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 chain2ygf 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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PDB2ygf Features of the Streptomyces Hygroscopicus Htpg Reveal How Partial Geldanamycin Resistance Can Arise by Mutation to the ATP Binding Pocket of a Eukaryotic Hsp90.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		N37 D40 A41 K44 D79 N92 K98 G121 V122 F124
Binding residue
(residue number reindexed from 1)		N36 D39 A40 K43 D78 N91 K97 G120 V121 F123
Annotation score1
Binding affinityMOAD: Kd~10uM
PDBbind-CN: -logKd/Ki=5.09,Kd=8.06uM
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:2ygf, PDBe:2ygf, PDBj:2ygf
PDBsum2ygf
PubMed21778327
UniProtP02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 (Gene Name=HSP82)

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