› 3t64

X-ray diffraction
1.65Å resolution

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

Assemblies composition:
hetero tetramer (preferred)
homo trimer
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-164064 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 181 amino acids
Theoretical weight: 20.63 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8II92 (Residues: 1-173; Coverage: 100%)
Gene name: PF3D7_1127100
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A
5'-(BENZHYDRYLAMINO)-2',5'-DIDEOXYURIDINE Chain: F
Molecule details ›
Chain: F
Length: 3 amino acids
Theoretical weight: 298 Da
Source organism: Escherichia coli

Ligands and Environments

2 bound ligands:
Ligand DU3 3 x DU3
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P41
Unit cell:
a: 77.01Å b: 77.01Å c: 106.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.19 0.216
Expression system: Escherichia coli

Quick links

Citations

2 review citations

From crystal to compound: structure-based antimalarial drug discovery.
Drinkwater et al. (2014)
1 more

6 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
5 more