› 2d00

X-ray diffraction
2.2Å resolution

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo hexamer (preferred)
homo dodecamer
Assembly name:
PDBe Complex ID:
PDB-CPX-159961 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
V-type ATP synthase subunit F Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 109 amino acids
Theoretical weight: 11.88 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: P74903 (Residues: 1-104; Coverage: 100%)
Gene names: TTHA1274, atpF, vatF
Sequence domains: ATP synthase (F/14-kDa) subunit
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA, ESRF BEAMLINE ID14-4
Spacegroup: P21212
Unit cell:
a: 81.705Å b: 138.295Å c: 66.096Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.262
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology.
Forgac M. (2007)
6 more

4 mentions without citation

Structure of the yeast vacuolar ATPase.
Zhang et al. (2008)
3 more