› 1dup

X-ray diffraction
1.9Å resolution

DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDO HYDROLASE (D-UTPASE)

Released:
DOI: 10.2210/pdb1dup/pdb
PDB entry 1dup coloured by chain, front view.
PDB entry 1dup coloured by chain, side view.
PDB entry 1dup coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of a dUTPase.
Cedergren-Zeppezauer ES, Larsson G, Nyman PO, Dauter Z, Wilson KS
Nature 355 740-3 (1992)
PMID: 1311056

Function and Biology Details

Reaction catalysed: 
dUTP + H(2)O = dUMP + diphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139313 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chain: A
Molecule details ›
Chain: A
Length: 152 amino acids
Theoretical weight: 16.3 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P06968 (Residues: 1-152; Coverage: 100%)
Gene names: JW3615, b3640, dnaS, dut, sof
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R3
Unit cell:
a: 86.61Å b: 86.61Å c: 62.27Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.15 not available not available

Quick links

Citations

6 review citations

DNA base damage recognition and removal: new twists and grooves.
Huffman et al. (2005)
5 more

6 mentions without citation

CHEK2 contribution to hereditary breast cancer in non-BRCA families.
Desrichard et al. (2011)
5 more