Structure of PDB 6cyh Chain A

Receptor sequence
>6cyhA (length=210) Species: 9606 (Homo sapiens) [Search protein sequence]
EVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLT
DPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGT
KAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESS
AGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIG
YPITLFVEKE
3D structure
PDB6cyh NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90.
ChainA
Resolution1.49 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 N5A A A55 M98 N106 T109 S113 Y139 A40 M83 N91 T94 S98 Y124 MOAD: Kd=708uM
PDBbind-CN: -logKd/Ki=3.15,Kd=708uM
BS02 MG A K69 N155 K54 N140
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

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6cyh, PDBe:6cyh, PDBj:6cyh
PDBsum6cyh
PubMed31501246
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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