› 6gdf

X-ray diffraction
2.5Å resolution

DIHYDROOROTASE FROM AQUIFEX AEOLICUS UNDER 600 BAR OF HYDROSTATIC PRESSURE

Released:
DOI: 10.2210/pdb6gdf/pdb
PDB entry 6gdf coloured by chain, front view.
PDB entry 6gdf coloured by chain, side view.
PDB entry 6gdf coloured by chain, top view.
Source organism: Aquifex aeolicus VF5
Primary publication:
Pressure-induced activation of latent dihydroorotase from Aquifex aeolicus as revealed by high pressure protein crystallography.
Prangé T, Girard E, Fourme R, Dhaussy AC, Edwards B, Vaishnav A, Patel C, Guy-Evans H, Hervé G, Evans DR
FEBS J 286 1204-1213 (2019)
PMID: 30657257

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130406 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotase Chain: A
Molecule details ›
Chain: A
Length: 423 amino acids
Theoretical weight: 46.63 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O66990 (Residues: 1-422; Coverage: 100%)
Gene names: aq_806, pyrC
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 1 x ZN
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID27
Spacegroup: C2221
Unit cell:
a: 90.84Å b: 176.488Å c: 65.518Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 not available
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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