Function and Biology Details
Reaction catalysed:
ATP + H(2)O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
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, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 548 amino acids
Theoretical weight: 57.42 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:
Length: 548 amino acids
Theoretical weight: 57.42 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P0A6F5 (Residues: 1-548; Coverage: 100%)
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:
Co-chaperonin GroES
Molecule details ›
Chains: 1, 2, O, P, Q, R, S, T, U, V, W, X, Y, Z
Length: 97 amino acids
Theoretical weight: 10.4 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Chaperonin 10 Kd subunit
Structure domains: GroES chaperonin
Length: 97 amino acids
Theoretical weight: 10.4 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P0A6F9 (Residues: 1-97; Coverage: 100%)
Sequence domains: Chaperonin 10 Kd subunit
Structure domains: GroES chaperonin
