Function and Biology Details
Reaction catalysed:
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero tetradecamer (preferred)
Assembly name:
Chaperonin GroEL and Co-chaperonin GroES (preferred)
PDBe Complex ID:
PDB-CPX-141323 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperonin GroEL
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 547 amino acids
Theoretical weight: 57.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: TCP-1/cpn60 chaperonin family
Length: 547 amino acids
Theoretical weight: 57.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P0A6F5 (Residues: 2-548; Coverage: 100%)
Sequence domains: TCP-1/cpn60 chaperonin family
Co-chaperonin GroES
Molecule details ›
Chains: O, P, Q, R, S, T, U
Length: 97 amino acids
Theoretical weight: 10.4 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Chaperonin 10 Kd subunit
Length: 97 amino acids
Theoretical weight: 10.4 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P0A6F9 (Residues: 1-97; Coverage: 100%)
Sequence domains: Chaperonin 10 Kd subunit
