› › Function and Biology

Cryo-EM structure of occupied ring subunit 1 (OR1) of GroEL from GroEL-UGT1A double occupied ring complex

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

Quick links

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 7xop contains 1 copy of Pfam domain PF00118 (TCP-1/cpn60 chaperonin family) in Chaperonin GroEL. Showing 1 copy in chain A [auth K].

Quick links