3jze

X-ray diffraction
1.8Å resolution

1.8 Angstrom resolution crystal structure of dihydroorotase (pyrC) from Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

Released:
Entry authors: Minasov G, Halavaty A, Shuvalova L, Dubrovska I, Winsor J, Papazisi L, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138927 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 372 amino acids
Theoretical weight: 41.44 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
Expression system: Escherichia coli
UniProt:
  • Canonical: P06204 (Residues: 1-348; Coverage: 100%)
Gene names: STM1163, pyrC
Sequence domains: Amidohydrolase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 50.437Å b: 79.486Å c: 180.61Å
α: 90° β: 90.35° γ: 90°
R-values:
R R work R free
0.165 0.163 0.203
Expression system: Escherichia coli