3hhq

X-ray diffraction
2Å resolution

Crystal structure of apo dUT1p from Saccharomyces cerevisiae

Released:

Function and Biology Details

Reaction catalysed:
dUTP + H(2)O = dUMP + diphosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-152587 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyuridine 5'-triphosphate nucleotidohydrolase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, X
Length: 167 amino acids
Theoretical weight: 17.49 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P33317 (Residues: 1-147; Coverage: 100%)
Gene names: DUT1, YBR1705, YBR252W
Sequence domains: dUTPase
Structure domains: Deoxyuridine 5'-Triphosphate Nucleotidohydrolase; Chain A

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P1
Unit cell:
a: 95.461Å b: 95.466Å c: 97.594Å
α: 98.79° β: 97.42° γ: 107.13°
R-values:
R R work R free
0.178 0.175 0.236
Expression system: Escherichia coli