› 2hqu

X-ray diffraction
2.2Å resolution

Human dUTPase in complex with alpha,beta-iminodUTP and magnesium ion

Released:
DOI: 10.2210/pdb2hqu/pdb
PDB entry 2hqu coloured by chain, front view.
PDB entry 2hqu coloured by chain, side view.
PDB entry 2hqu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase.
Varga B, Barabás O, Kovári J, Tóth J, Hunyadi-Gulyás E, Klement E, Medzihradszky KF, Tölgyesi F, Fidy J, Vértessy BG
FEBS Lett 581 4783-8 (2007)
PMID: 17880943

Function and Biology Details

Reaction catalysed: 
dUTP + H(2)O = dUMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152585 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 164 amino acids
Theoretical weight: 17.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P33316 (Residues: 94-252; Coverage: 63%)
Gene name: DUT
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

3 bound ligands:
Ligand MG 4 x MG
Ligand DUP 3 x DUP
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 65.409Å b: 71.773Å c: 76.475Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.251
Expression system: Escherichia coli BL21

Quick links

Citations

3 review citations

A survey of the year 2007 literature on applications of isothermal titration calorimetry.
Bjelić et al. (2008)
2 more

17 mentions without citation

Keeping uracil out of DNA: physiological role, structure and catalytic mechanism of dUTPases.
Vértessy et al. (2009)
16 more