› 2we1

X-ray diffraction
1.8Å resolution

EBV dUTPase mutant Asp131Asn with bound dUMP

Released:
DOI: 10.2210/pdb2we1/pdb
PDB entry 2we1 coloured by chain, front view.
PDB entry 2we1 coloured by chain, side view.
PDB entry 2we1 coloured by chain, top view.
Source organism: Human herpesvirus 4 strain B95-8
Primary publication:
The flexible motif V of Epstein-Barr virus deoxyuridine 5'-triphosphate pyrophosphatase is essential for catalysis.
Freeman L, Buisson M, Tarbouriech N, Van der Heyden A, Labbé P, Burmeister WP
J Biol Chem 284 25280-9 (2009)
PMID: 19586911

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136646 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 31.66 KDa
Source organism: Human herpesvirus 4 strain B95-8
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P03195 (Residues: 1-278; Coverage: 100%)
Gene names: BLLF3, DUT
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

2 bound ligands:
Ligand UMP 1 x UMP
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 55.624Å b: 56.859Å c: 81.073Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.247
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

dUTPases, the unexplored family of signalling molecules.
Penadés et al. (2013)
18 other articles

1 mention without citation

The flexible motif V of Epstein-Barr virus deoxyuridine 5'-triphosphate pyrophosphatase is essential for catalysis.
Freeman et al. (2009)