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:
- V-type ATP synthase regulatory subunit B/beta
- P-loop containing nucleoside triphosphate hydrolase
- 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
- V-type ATP synthase catalytic alpha chain
- ATPase, F1/V1 complex, beta/alpha subunit, C-terminal
- ATPsynthase alpha/beta subunit, N-terminal extension
2 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
V-type ATP synthase (preferred)
PDBe Complex ID:
PDB-CPX-176369 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
V-type ATP synthase alpha chain
Molecule details ›
Chains: A, C
Length: 578 amino acids
Theoretical weight: 63.64 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 578 amino acids
Theoretical weight: 63.64 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
- Canonical:
Q56403 (Residues: 1-578; Coverage: 100%)
Sequence domains:
- ATP synthase alpha/beta family, beta-barrel domain
- ATPsynthase alpha/beta subunit N-term extension
- ATP synthase alpha/beta family, nucleotide-binding domain
V-type ATP synthase beta chain
Molecule details ›
Chains: B, D
Length: 464 amino acids
Theoretical weight: 51.62 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 464 amino acids
Theoretical weight: 51.62 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
- Canonical: Q56404 (Residues: 1-464; Coverage: 97%)
Sequence domains:
- ATP synthase alpha/beta family, beta-barrel domain
- ATP synthase alpha/beta family, nucleotide-binding domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-2
Spacegroup:
P321
Expression system: Escherichia coli
