› 4heb

X-ray diffraction
2.26Å resolution

Function and Biology Details

Reaction catalysed: 
A nucleoside triphosphate + H(2)O = a nucleotide + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169680 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
dTTP/UTP pyrophosphatase Chains: A, B
Molecule details ›
Chains: A, B
Length: 210 amino acids
Theoretical weight: 23.75 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02169 (Residues: 1-189; Coverage: 100%)
Gene names: BSU28050, maf
Sequence domains: Maf-like protein
Structure domains: Maf protein

Ligands and Environments

1 bound ligand:
Ligand UNX 31 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 61.55Å b: 85.95Å c: 95.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.215 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Preventive DNA repair by sanitizing the cellular (deoxy)nucleoside triphosphate pool.
Nagy et al. (2014)
9 other articles

2 mentions without citation

Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.
Tchigvintsev et al. (2013)
1 more