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-242116 (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: 528 amino acids
Theoretical weight: 56.08 KDa
Source organism: Hydrogenophilus thermoluteolus
UniProt:
Sequence domains: TCP-1/cpn60 chaperonin family
Length: 528 amino acids
Theoretical weight: 56.08 KDa
Source organism: Hydrogenophilus thermoluteolus
UniProt:
- Canonical:
A0A2Z6DW38 (Residues: 2-529; Coverage: 97%)
Sequence domains: TCP-1/cpn60 chaperonin family
Co-chaperonin GroES
Molecule details ›
Chains: a, b, c, d, e, f, g, h, i, j, k, l, m, n
Length: 94 amino acids
Theoretical weight: 10.22 KDa
Source organism: Hydrogenophilus thermoluteolus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Chaperonin 10 Kd subunit
Length: 94 amino acids
Theoretical weight: 10.22 KDa
Source organism: Hydrogenophilus thermoluteolus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: A0A2Z6DVV7 (Residues: 2-95; Coverage: 98%)
Sequence domains: Chaperonin 10 Kd subunit
