Structure of PDB 6cyg Chain A

Receptor sequence
>6cygA (length=210) Species: 9606 (Homo sapiens) [Search protein sequence]
EVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLT
DPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGT
KAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESS
AGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIG
YPITLFVEKE
3D structure
PDB6cyg NECA derivatives exploit the paralog-specific properties of the site 3 side pocket of Grp94, the endoplasmic reticulum Hsp90.
ChainA
Resolution1.50392 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 N5O A A55 M98 N106 G135 V136 Y139 A40 M83 N91 G120 V121 Y124 MOAD: Kd=68uM
PDBbind-CN: -logKd/Ki=4.17,Kd=67.5uM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6cyg, PDBe:6cyg, PDBj:6cyg
PDBsum6cyg
PubMed31501246
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

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