Structure of PDB 2byh Chain A

Receptor sequence
>2byhA (length=215) Species: 9606 (Homo sapiens) [Search protein sequence]
PMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIR
YESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTI
AKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQY
AWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKH
SQFIGYPITLFVEKE
3D structure
PDB2byh 3-(5-Chloro-2,4-Dihydroxyphenyl)-Pyrazole-4-Carboxamides as Inhibitors of the Hsp90 Molecular Chaperone.
ChainA
Resolution1.9 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 2D7 A N51 A55 D93 G97 M98 N106 G135 V136 F138 T184 N41 A45 D83 G87 M88 N96 G125 V126 F128 T174 MOAD: ic50=0.258uM
PDBbind-CN: -logKd/Ki=6.59,IC50=0.258uM
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:2byh, PDBe:2byh, PDBj:2byh
PDBsum2byh
PubMed16213716
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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