› 4ooq

X-ray diffraction
2Å 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-193534 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 166 amino acids
Theoretical weight: 17.58 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9STG6 (Residues: 1-166; Coverage: 100%)
Gene names: At3g46940, DUT, DUT1, T6H20.30
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 69.939Å b: 70.621Å c: 75.001Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.148 0.196
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Crystal Structure of African Swine Fever Virus dUTPase Reveals a Potential Drug Target.
Li et al. (2019)
4 more

1 mention without citation

Structural insights into the mechanism defining substrate affinity in Arabidopsis thaliana dUTPase: the role of tryptophan 93 in ligand orientation.
Inoguchi et al. (2015)