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 21-mer (preferred)
Assembly name:
GroEL-GroES complex (preferred)
PDBe Complex ID:
PDB-CPX-141318 (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: 526 amino acids
Theoretical weight: 55.46 KDa
Source organism: Escherichia coli BL21
Expression system: Escherichia coli
UniProt:
Sequence domains: TCP-1/cpn60 chaperonin family
Length: 526 amino acids
Theoretical weight: 55.46 KDa
Source organism: Escherichia coli BL21
Expression system: Escherichia coli
UniProt:
- Canonical:
P0A6F5 (Residues: 2-527; Coverage: 96%)
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 K-12
Expression system: Escherichia coli
UniProt:
Sequence domains: Chaperonin 10 Kd subunit
Length: 97 amino acids
Theoretical weight: 10.4 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
- Canonical: P0A6F9 (Residues: 1-97; Coverage: 100%)
Sequence domains: Chaperonin 10 Kd subunit
