› 6mai

X-ray diffraction
1.8Å resolution

Crystal structure of Deoxyuridine 5'-triphosphate nucleotidohydrolase from Legionella pneumophila Philadelphia 1

Released:
DOI: 10.2210/pdb6mai/pdb
Model geometry
Fit model/data
PDB entry 6mai coloured by chain, front view.
PDB entry 6mai coloured by chain, side view.
PDB entry 6mai coloured by chain, top view.
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Primary publication:
Structural characterization of dUTPase from Legionella pneumophila
Nguyen CL, Tramell AR, Norman JO, Abendroth J, Barrett KF, Craig JK, Edwards TE, Lorimer DD, McLaughlin KJ
Acta Crystallogr F Struct Biol Commun 81 155-162 (2025)

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-178596 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chain: A
Molecule details ›
Chain: A
Length: 160 amino acids
Theoretical weight: 17.39 KDa
Source organism: Legionella pneumophila subsp. pneumophila str. Philadelphia 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5ZSN0 (Residues: 1-152; Coverage: 100%)
Gene names: dut, lpg2487
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

1 bound ligand:
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P63
Unit cell:
a: 84.65Å b: 84.65Å c: 55.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.156 0.154 0.177
Expression system: Escherichia coli BL21(DE3)

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