Structure of PDB 7ry1 Chain C

Receptor sequence
>7ry1C (length=406) Species: 9606 (Homo sapiens) [Search protein sequence]
TKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLF
VPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSE
DLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFS
KNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIY
YITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLV
SVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRL
VTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSI
IETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMI
KLGLGI
3D structure
PDB7ry1 Crystal structure of the middle and C-terminal domains of Hsp90 alpha labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target.
ChainC
Resolution3.523 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 MDC C M371 C374 E375 Q405 L409 M79 C82 E83 Q113 L117
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:7ry1, PDBe:7ry1, PDBj:7ry1
PDBsum7ry1
PubMed35503206
UniProtP07900|HS90A_HUMAN Heat shock protein HSP 90-alpha (Gene Name=HSP90AA1)

[Back to BioLiP]