› 1dud

X-ray diffraction
2.3Å resolution

DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDE HYDROLASE (D-UTPASE) COMPLEXED WITH THE SUBSTRATE ANALOGUE DEOXYURIDINE 5'-DIPHOSPHATE (D-UDP)

Released:
DOI: 10.2210/pdb1dud/pdb
PDB entry 1dud coloured by chain, front view.
PDB entry 1dud coloured by chain, side view.
PDB entry 1dud coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP).
Larsson G, Svensson LA, Nyman PO
Nat Struct Biol 3 532-8 (1996)
PMID: 8646539

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

1 bound ligand:
Ligand DUD 1 x DUD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: R3
Unit cell:
a: 86.64Å b: 86.64Å c: 62.23Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.2 not available

Quick links

Citations

3 review citations

3D domain swapping: as domains continue to swap.
Liu et al. (2002)
2 more