2ol1

X-ray diffraction
1.8Å resolution

High Resolution Crystal Structures of Vaccinia Virus dUTPase

Released:
Source organism: Vaccinia virus
Primary publication:
Structures of vaccinia virus dUTPase and its nucleotide complexes.
Acta Crystallogr D Biol Crystallogr 63 571-80 (2007)
PMID: 17452782

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-148044 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 147 amino acids
Theoretical weight: 16.32 KDa
Source organism: Vaccinia virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P17374 (Residues: 1-147; Coverage: 100%)
Gene names: DUT, F2L, OPG046, VACWR041
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P65
Unit cell:
a: 119.97Å b: 119.97Å c: 50.13Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.199 0.231
Expression system: Escherichia coli