Structure of PDB 2qg0 Chain A

Receptor sequence
>2qg0A (length=207) Species: 9606 (Homo sapiens) [Search protein sequence]
VETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTD
PSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTK
AFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSA
GGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGY
PITLFVE
3D structure
PDB2qg0 Discovery and design of novel HSP90 inhibitors using multiple fragment-based design strategies.
ChainA
Resolution1.85 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 A94 A N51 D54 A55 I96 G97 M98 N106 G135 V136 F138 N35 D38 A39 I80 G81 M82 N90 G119 V120 F122 MOAD: Ki=1.9uM
PDBbind-CN: -logKd/Ki=5.72,Ki=1.9uM
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
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Biological Process
External links
PDB RCSB:2qg0, PDBe:2qg0, PDBj:2qg0
PDBsum2qg0
PubMed17630989
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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