PDBe 1f48

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF THE ESCHERICHIA COLI ARSENITE-TRANSLOCATING ATPASE

Released:

Function and Biology Details

Reaction catalysed:
ATP + H(2)O + arsenite(In) = ADP + phosphate + arsenite(Out). 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arsenical pump-driving ATPase Chain: A
Molecule details ›
Chain: A
Length: 589 amino acids
Theoretical weight: 64.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08690 (Residues: 1-583; Coverage: 100%)
Gene name: arsA
Sequence domains: Anion-transporting ATPase
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I222
Unit cell:
a: 73.523Å b: 75.715Å c: 222.714Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.263
Expression system: Escherichia coli