› 3mpg

X-ray diffraction
2.6Å resolution

Dihydroorotase from Bacillus anthracis

Released:
DOI: 10.2210/pdb3mpg/pdb
PDB entry 3mpg coloured by chain, front view.
PDB entry 3mpg coloured by chain, side view.
PDB entry 3mpg coloured by chain, top view.
Source organism: Bacillus anthracis
Primary publication:
Structure of dihydroorotase from Bacillus anthracis at 2.6 Å resolution.
Mehboob S, Mulhearn DC, Truong K, Johnson ME, Santarsiero BD
Acta Crystallogr Sect F Struct Biol Cryst Commun 66 1432-5 (2010)
PMID: 21045288

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182613 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotase Chains: A, B
Molecule details ›
Chains: A, B
Length: 428 amino acids
Theoretical weight: 46.72 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q81WF0 (Residues: 1-428; Coverage: 100%)
Gene names: BAS3739, BA_4027, GBAA_4027, pyrC
Sequence domains: Amidohydrolase family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 50.36Å b: 80.784Å c: 104.772Å
α: 90° β: 100.21° γ: 90°
R-values:
R R work R free
0.212 0.212 0.293
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD.
Grande-García et al. (2014)
4 more

9 mentions without citation

The Blueprint of a Minimal Cell: MiniBacillus.
Reuß et al. (2016)
8 more