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Structure of the GroEL-ATP complex plunge-frozen 13 ms after mixing with ATP

Source organism: Escherichia coli
Biochemical function: ATP-dependent protein folding chaperone
Biological process: chaperone cofactor-dependent protein refolding
Cellular component: GroEL-GroES complex

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EC 5.6.1.7: Chaperonin ATPase

Reaction catalysed:
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Systematic name:
ATP phosphohydrolase (polypeptide-unfolding)
Alternative Name(s):
  • Chaperonin

GO terms

Sequence family

Pfam Protein family (Pfam)
PF00118
Domain description: TCP-1/cpn60 chaperonin family
Occurring in:
  1. Chaperonin GroEL
The deposited structure of PDB entry 8bly contains 14 copies of Pfam domain PF00118 (TCP-1/cpn60 chaperonin family) in Chaperonin GroEL. Showing 1 copy in chain A.

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