› 3d6n

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reactions catalysed: 
(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero dodecamer
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130368 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dihydroorotase Chain: A
Molecule details ›
Chain: A
Length: 422 amino acids
Theoretical weight: 46.44 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O66990 (Residues: 1-422; Coverage: 100%)
Gene names: aq_806, pyrC
Sequence domains: Amidohydrolase family
Structure domains:
Aspartate carbamoyltransferase catalytic subunit Chain: B
Molecule details ›
Chain: B
Length: 291 amino acids
Theoretical weight: 33.61 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O66726 (Residues: 1-291; Coverage: 100%)
Gene names: aq_409, pyrB
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand FLC 2 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: R32
Unit cell:
a: 158.439Å b: 158.439Å c: 233.553Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.164 0.204
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Sources and Fates of Carbamyl Phosphate: A Labile Energy-Rich Molecule with Multiple Facets.
Shi et al. (2018)
2 more

8 mentions without citation

Deciphering CAD: Structure and function of a mega-enzymatic pyrimidine factory in health and disease.
Del Caño-Ochoa et al. (2021)
7 more