Function and Biology Details
Reaction catalysed:
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero 28-mer (preferred)
Assembly name:
Co-chaperonin GroES and Chaperonin GroEL (preferred)
PDBe Complex ID:
PDB-CPX-141316 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Chaperonin GroEL
Molecule details ›
Chains: A, BA, C, E, G, I, K, M, O, Q, S, V, X, Z
Length: 548 amino acids
Theoretical weight: 57.39 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: TCP-1/cpn60 chaperonin family
Length: 548 amino acids
Theoretical weight: 57.39 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P0A6F5 (Residues: 1-548; Coverage: 100%)
Sequence domains: TCP-1/cpn60 chaperonin family
Co-chaperonin GroES
Molecule details ›
Chains: AA, B, CA, D, F, H, J, L, N, P, R, T, W, Y
Length: 96 amino acids
Theoretical weight: 10.27 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains: Chaperonin 10 Kd subunit
Length: 96 amino acids
Theoretical weight: 10.27 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: P0A6F9 (Residues: 2-97; Coverage: 99%)
Sequence domains: Chaperonin 10 Kd subunit
