3ehw

X-ray diffraction
1.8Å resolution

Human dUTPase in complex with alpha,beta-imido-dUTP and Mg2+: visualization of the full-length C-termini in all monomers and suggestion for an additional metal ion binding site

Released:
Source organism: Homo sapiens
Entry authors: Takacs E, Barabas O, Vertessy BG

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-152585 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial Chains: A, B, C, X, Y, Z
Molecule details ›
Chains: A, B, C, X, Y, Z
Length: 164 amino acids
Theoretical weight: 17.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 65.446Å b: 87.16Å c: 70.608Å
α: 90° β: 90.09° γ: 90°
R-values:
R R work R free
0.16 0.158 0.199
Expression system: Escherichia coli BL21(DE3)