› › Function and Biology

In situ structure average of GroEL14-GroES14 complexes in Escherichia coli cytosol obtained by cryo electron tomography

Source organism: Escherichia coli BL21(DE3)
Biochemical function: unfolded protein binding
Biological process: protein folding
Cellular component: cytoplasm

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

Biochemical function:
Biological process:
Cellular component:

Sequence families

Pfam Protein families (Pfam)
PF00166
Domain description: Chaperonin 10 Kd subunit
Occurring in:
  1. Co-chaperonin GroES
The deposited structure of PDB entry 8p4r contains 14 copies of Pfam domain PF00166 (Chaperonin 10 Kd subunit) in Co-chaperonin GroES. Showing 1 copy in chain H [auth O].

PF00118
Domain description: TCP-1/cpn60 chaperonin family
Occurring in:
  1. Chaperonin GroEL
The deposited structure of PDB entry 8p4r contains 14 copies of Pfam domain PF00118 (TCP-1/cpn60 chaperonin family) in Chaperonin GroEL. Showing 1 copy in chain A.

Quick links