Structure of PDB 3hyz Chain B Binding Site BS01

Receptor Information
>3hyz Chain B (length=209) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
EVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLT
DPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGT
KAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESS
AGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIG
YPITLFVEK
Ligand information
Ligand ID42C
InChIInChI=1S/C7H9N5/c1-12(2)7-5-6(9-3-8-5)10-4-11-7/h3-4H,1-2H3,(H,8,9,10,11)
InChIKeyBVIAOQMSVZHOJM-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04n1c(c2c(nc1)ncn2)N(C)C
OpenEye OEToolkits 1.5.0CN(C)c1c2c(nc[nH]2)ncn1
CACTVS 3.341CN(C)c1ncnc2nc[nH]c12
FormulaC7 H9 N5
NameN,N-dimethyl-7H-purin-6-amine
ChEMBLCHEMBL407391
DrugBank
ZINCZINC000013516321
PDB chain3hyz Chain B Residue 237 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3hyz Crystal structure of Hsp90 with fragment 42-C03
Resolution2.3 Å
Binding residue
(original residue number in PDB)		N51 A55 D93 M98 T184
Binding residue
(residue number reindexed from 1)		N36 A40 D78 M83 T169
Annotation score1
Enzymatic activity
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
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:3hyz, PDBe:3hyz, PDBj:3hyz
PDBsum3hyz
PubMed
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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