› 3i93

X-ray diffraction
1.8Å resolution

Crystal structure of Mycobacterium tuberculosis dUTPase STOP138T mutant

Released:
DOI: 10.2210/pdb3i93/pdb
PDB entry 3i93 coloured by chain, front view.
PDB entry 3i93 coloured by chain, side view.
PDB entry 3i93 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases.
Takács E, Nagy G, Leveles I, Harmat V, Lopata A, Tóth J, Vértessy BG
FEBS Lett 584 3047-54 (2010)
PMID: 20493855

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-161882 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 16.57 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WNS5 (Residues: 1-138; Coverage: 90%)
Gene names: MTCY05A6.18c, Rv2697c, dut
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand DUP 1 x DUP
Ligand TRS 2 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P63
Unit cell:
a: 54.591Å b: 54.591Å c: 83.051Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.164 0.206
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

The dUTPase enzyme is essential in Mycobacterium smegmatis.
Pecsi et al. (2012)
10 more

1 mention without citation

Direct contacts between conserved motifs of different subunits provide major contribution to active site organization in human and mycobacterial dUTPases.
Takács et al. (2010)