Structure of PDB 2qg2 Chain A

Receptor sequence
>2qg2A (length=207) Species: 9606 (Homo sapiens) [Search protein sequence]
VETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYETLTD
PSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTK
AFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSA
GGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGY
PITLFVE
3D structure
PDB2qg2 Discovery and design of novel HSP90 inhibitors using multiple fragment-based design strategies.
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.10: non-chaperonin molecular chaperone ATPase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 A91 A A55 G97 L103 L107 F138 W162 A39 G81 L87 L91 F122 W146 MOAD: Ki=4uM
PDBbind-CN: -logKd/Ki=5.40,Ki=4.0uM
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:2qg2, PDBe:2qg2, PDBj:2qg2
PDBsum2qg2
PubMed17630989
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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