5ynz

X-ray diffraction
2.77Å resolution

Crystal structure of the dihydroorotase domain (K1556A) of human CAD

Released:
Model geometry
Fit model/data

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-151061 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Multifunctional protein CAD Chain: A
Molecule details ›
Chain: A
Length: 391 amino acids
Theoretical weight: 42.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P27708 (Residues: 1456-1846; Coverage: 18%)
Gene name: CAD
Sequence domains: Amidohydrolase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: C222
Unit cell:
a: 88.841Å b: 108.63Å c: 99.219Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.226 0.289
Expression system: Escherichia coli BL21