Function and Biology Details
Reaction catalysed:
ATP + H(2)O + 4 H(+)(Side 1) = ADP + phosphate + 4 H(+)(Side 2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- P-loop containing nucleoside triphosphate hydrolase
- ATP synthase, F1 complex, alpha subunit
- ATP synthase, F1 complex, gamma subunit
- ATP synthase, F1 complex, beta subunit
- ATP synthase, alpha subunit, C-terminal
- ATPase, alpha/beta subunit, nucleotide-binding domain, active site
- ATPase, F1/V1/A1 complex, alpha/beta subunit, nucleotide-binding domain
- ATPase, F1/V1/A1 complex, alpha/beta subunit, N-terminal domain
8 more domains
Structure analysis Details
Assembly composition:
hetero heptamer (preferred)
Assembly name:
ATP synthase, complex V (preferred)
PDBe Complex ID:
PDB-CPX-133625 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
ATP synthase subunit alpha, mitochondrial
Molecule details ›
Chains: A, B, C
Length: 553 amino acids
Theoretical weight: 59.8 KDa
Source organism: Bos taurus
UniProt:
Sequence domains:
Length: 553 amino acids
Theoretical weight: 59.8 KDa
Source organism: Bos taurus
UniProt:
- Canonical:
P19483 (Residues: 1-553; Coverage: 100%)
Sequence domains:
ATP synthase subunit beta, mitochondrial
Molecule details ›
Chains: D, E, F
Length: 528 amino acids
Theoretical weight: 56.34 KDa
Source organism: Bos taurus
UniProt:
Sequence domains:
Length: 528 amino acids
Theoretical weight: 56.34 KDa
Source organism: Bos taurus
UniProt:
- Canonical: P00829 (Residues: 1-528; Coverage: 100%)
Sequence domains:
ATP synthase subunit gamma, mitochondrial
Molecule details ›
Chain: G
Length: 298 amino acids
Theoretical weight: 33.12 KDa
Source organism: Bos taurus
UniProt:
Sequence domains: ATP synthase
Length: 298 amino acids
Theoretical weight: 33.12 KDa
Source organism: Bos taurus
UniProt:
- Canonical: P05631 (Residues: 1-298; Coverage: 100%)
Sequence domains: ATP synthase
