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:
PDBe Complex ID:
PDB-CPX-145457 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
60 kDa heat shock protein, mitochondrial
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 558 amino acids
Theoretical weight: 59.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli-Thermus thermophilus shuttle vector pTRH1T
UniProt:
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:
Length: 558 amino acids
Theoretical weight: 59.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli-Thermus thermophilus shuttle vector pTRH1T
UniProt:
- Canonical:
P10809 (Residues: 27-556; Coverage: 93%)
Sequence domains: TCP-1/cpn60 chaperonin family
Structure domains:
10 kDa heat shock protein, mitochondrial
Molecule details ›
Chains: 1, 2, O, P, Q, R, S, T, U, V, W, X, Y, Z
Length: 114 amino acids
Theoretical weight: 12.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli-Thermus thermophilus shuttle vector pTRH1T
UniProt:
Sequence domains: Chaperonin 10 Kd subunit
Structure domains: GroES chaperonin
Length: 114 amino acids
Theoretical weight: 12.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli-Thermus thermophilus shuttle vector pTRH1T
UniProt:
- Canonical: P61604 (Residues: 1-102; Coverage: 100%)
Sequence domains: Chaperonin 10 Kd subunit
Structure domains: GroES chaperonin
