3mbq

X-ray diffraction
2.1Å resolution

Crystal structure of deoxyuridine 5-triphosphate nucleotidohydrolase from Brucella melitensis, orthorhombic crystal form

Released:
Source organism: Brucella abortus 2308
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

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-174207 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 178 amino acids
Theoretical weight: 18.97 KDa
Source organism: Brucella abortus 2308
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2YRG4 (Residues: 1-157; Coverage: 100%)
Gene names: BAB1_1687, dut
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: ALS BEAMLINE 5.0.1
Spacegroup: P212121
Unit cell:
a: 50.56Å b: 95.89Å c: 100.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.166 0.208
Expression system: Escherichia coli