Structure of PDB 3ekr Chain A

Receptor sequence
>3ekrA (length=217) Species: 9606 (Homo sapiens) [Search protein sequence]
QPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKI
RYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGT
IAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQ
YAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKK
HSQFIGYPITLFVEKEL
3D structure
PDB3ekr Dihydroxylphenyl amides as inhibitors of the Hsp90 molecular chaperone.
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 PY9 A N51 A55 K58 D93 I96 G97 M98 T184 N42 A46 K49 D84 I87 G88 M89 T175 MOAD: Ki=0.03uM
PDBbind-CN: -logKd/Ki=7.52,Ki=0.03uM
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
View graph for
Biological Process
External links
PDB RCSB:3ekr, PDBe:3ekr, PDBj:3ekr
PDBsum3ekr
PubMed18929486
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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