Structure of PDB 2yeg Chain B Binding Site BS01

Receptor Information

>2yeg Chain B (length=208) 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
YPITLFVE

Ligand information

Ligand ID

XQG

InChI

InChI=1S/C6H6N4S/c1-11-6-4-5(8-2-7-4)9-3-10-6/h2-3H,1H3,(H,7,8,9,10)

InChIKey

UIJIQXGRFSPYQW-UHFFFAOYSA-N

SMILES

Software	SMILES
CACTVS 3.352	CSc1ncnc2[nH]cnc12
OpenEye OEToolkits 1.6.1	CSc1c2c([nH]cn2)ncn1

Formula

C6 H6 N4 S

Name

6-METHYLSULFANYL-9H-PURINE

PDB chain

2yeg Chain B Residue 1224 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2yeg How Well Can Fragments Explore Accessed Chemical Space? a Case Study from Heat Shock Protein 90.
Resolution	2.5 Å
Binding residue (original residue number in PDB)	A55 D93 M98 T184 E223
Binding residue (residue number reindexed from 1)	A40 D78 M83 T169 E208
Annotation score	1

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:2yeg, PDBe:2yeg, PDBj:2yeg
PDBsum	2yeg
PubMed	21561141
UniProt	P07900\|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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