› 5cco

X-ray diffraction
2.33Å resolution

Function and Biology Details

Reaction catalysed: 
dUTP + H(2)O = dUMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107512 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dUTP diphosphatase Chain: A
Molecule details ›
Chain: A
Length: 170 amino acids
Theoretical weight: 19.11 KDa
Source organism: Staphylococcus virus 80alpha
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A4ZF98 (Residues: 1-170; Coverage: 100%)
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

2 bound ligands:
Ligand UMP 1 x UMP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P213
Unit cell:
a: 87Å b: 87Å c: 87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.201 0.244
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 citation in other articles

Pirating conserved phage mechanisms promotes promiscuous staphylococcal pathogenicity island transfer.
Bowring et al. (2017)
14 more

1 mention without citation

Another look at the mechanism involving trimeric dUTPases in Staphylococcus aureus pathogenicity island induction involves novel players in the party.
Maiques et al. (2016)