› 1q5h

X-ray diffraction
2Å resolution

Human dUTP Pyrophosphatase complex with dUDP

Released:
DOI: 10.2210/pdb1q5h/pdb
PDB entry 1q5h coloured by chain, front view.
PDB entry 1q5h coloured by chain, side view.
PDB entry 1q5h coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits.
Mol CD, Harris JM, McIntosh EM, Tainer JA
Structure 4 1077-92 (1996)
PMID: 8805593

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152585 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 147 amino acids
Theoretical weight: 16.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P33316 (Residues: 112-252; Coverage: 56%)
Gene name: DUT
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand DUD 3 x DUD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 73.197Å b: 110.766Å c: 53.243Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.177 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

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

11 mentions without citation

Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins.
Németh-Pongrácz et al. (2007)
10 more