X-ray diffraction
2.8Å resolution

Human Dihydropyrimidinase

Source organism: Homo sapiens
Entry authors: Welin M, Karlberg T, Andersson J, Arrowsmith CH, Berglund H, Busam RD, Collins R, Dahlgren LG, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Herman MD, Johansson I, Kallas A, Kotenyova T, Lehtio L, Moche M, Nilsson ME, Nyman T, Persson C, Sagemark J, Svensson L, Thorsell AG, Tresaugues L, Van Den Berg S, Weigelt J, Wikstrom M, Nordlund P, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
5,6-dihydrouracil + H(2)O = 3-ureidopropanoate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Dihydropyrimidinase Chain: A
Molecule details ›
Chain: A
Length: 541 amino acids
Theoretical weight: 59.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q14117 (Residues: 1-519; Coverage: 100%)
Gene name: DPYS
Sequence domains: Amidohydrolase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P6422
Unit cell:
a: 89.65Å b: 89.65Å c: 219.1Å
α: 90° β: 90° γ: 120°
R R work R free
0.203 0.2 0.251
Expression system: Escherichia coli BL21(DE3)