Structure of PDB 1byq Chain A

Receptor sequence
>1byqA (length=213) Species: 9606 (Homo sapiens) [Search protein sequence]
PMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIR
YETLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTI
AKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQY
AWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKH
SQFIGYPITLFVE
3D structure
PDB1byq In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.
ChainA
Resolution1.5 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 ADP A N51 A55 M98 N106 F138 N41 A45 M88 N96 F128
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:1byq, PDBe:1byq, PDBj:1byq
PDBsum1byq
PubMed9817749
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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