3ca9

X-ray diffraction
3Å resolution

Evolution of chlorella virus dUTPase

Released:
Primary publication:
Crystallization and crystal-packing studies of Chlorella virus deoxyuridine triphosphatase.
Acta Crystallogr Sect F Struct Biol Cryst Commun 65 1030-4 (2009)
PMID: 19851015

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-177245 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dUTP diphosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 17.54 KDa
Source organism: Paramecium bursaria Chlorella virus IL3A
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5I3E5 (Residues: 1-141; Coverage: 100%)
Gene names: IL-3A_613L, PBCVIL3A_613L
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P213
Unit cell:
a: 105.647Å b: 105.647Å c: 105.647Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.232 0.307
Expression system: Escherichia coli