› 3tqz

X-ray diffraction
1.75Å resolution

Structure of a deoxyuridine 5'-triphosphate nucleotidohydrolase (dut) from Coxiella burnetii

Released:
DOI: 10.2210/pdb3tqz/pdb
PDB entry 3tqz coloured by chain, front view.
PDB entry 3tqz coloured by chain, side view.
PDB entry 3tqz coloured by chain, top view.
Source organism: Coxiella burnetii
Primary publication:
Structural genomics for drug design against the pathogen Coxiella burnetii.
Franklin MC, Cheung J, Rudolph MJ, Burshteyn F, Cassidy M, Gary E, Hillerich B, Yao ZK, Carlier PR, Totrov M, Love JD
Proteins 83 2124-36 (2015)
PMID: 26033498

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

Assemblies composition:
homo trimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175085 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 16.6 KDa
Source organism: Coxiella burnetii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q45920 (Residues: 1-152; Coverage: 100%)
Gene names: CBU_0293, dut
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
1 modified residue:
Ligand MSE 2 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P63
Unit cell:
a: 85.065Å b: 85.065Å c: 54.76Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.176 0.175 0.186
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology.
Martins et al. (2015)
4 more