Structure of PDB 3bmy Chain A

Receptor sequence
>3bmyA (length=213) Species: 9606 (Homo sapiens) [Search protein sequence]
QPMEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIR
YESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTI
AKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQY
AWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKH
SQFIGYPITLFVE
3D structure
PDB3bmy Discovery of benzisoxazoles as potent inhibitors of chaperone heat shock protein 90.
ChainA
Resolution1.6 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 CXZ A N51 A55 D93 I96 G97 M98 F138 T184 N41 A45 D83 I86 G87 M88 F128 T174 MOAD: ic50=0.03uM
PDBbind-CN: -logKd/Ki=7.52,IC50=0.03uM
BindingDB: IC50=30nM
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:3bmy, PDBe:3bmy, PDBj:3bmy
PDBsum3bmy
PubMed18197612
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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