X-ray diffraction
1.45Å resolution

Crystal structure of the dihydroorotase domain of human CAD in apo- form obtained recombinantly from HEK293 cells.


Function and Biology Details

Reactions catalysed:
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
CAD protein Chain: A
Molecule details ›
Chain: A
Length: 393 amino acids
Theoretical weight: 42.92 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
  • Canonical: P27708 (Residues: 1456-1846; Coverage: 18%)
Gene name: CAD
Sequence domains: Amidohydrolase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 82.11Å b: 158.8Å c: 60.76Å
α: 90° β: 90° γ: 90°
R R work R free
0.124 0.122 0.148
Expression system: Homo sapiens