Structure of PDB 2vci Chain A

Receptor sequence
>2vciA (length=208) Species: 9606 (Homo sapiens) [Search protein sequence]
EVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLT
DPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGT
KAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESS
AGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIG
YPITLFVE
3D structure
PDB2vci 4,5-diarylisoxazole Hsp90 chaperone inhibitors: potential therapeutic agents for the treatment of cancer.
ChainA
Resolution2.0 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 2GJ A N51 A55 K58 D93 I96 G97 M98 L107 T109 F138 T184 E223 N36 A40 K43 D78 I81 G82 M83 L92 T94 F123 T169 E208 MOAD: ic50=0.021uM
PDBbind-CN: -logKd/Ki=7.68,IC50=21nM
BindingDB: IC50=61nM,EC50=7nM,Ki=9nM
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:2vci, PDBe:2vci, PDBj:2vci
PDBsum2vci
PubMed18020435
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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