6cty

X-ray diffraction
2.41Å resolution

Crystal structure of dihydroorotase pyrC from Yersinia pestis in complex with zinc and malate at 2.4 A resolution

Released:

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 dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187197 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 372 amino acids
Theoretical weight: 41.41 KDa
Source organism: Yersinia pestis
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8ZFU4 (Residues: 1-348; Coverage: 100%)
Gene names: YPO1587, YP_2265, pyrC, y1746
Sequence domains: Amidohydrolase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 95.838Å b: 112.202Å c: 208.264Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.159 0.198
Expression system: Escherichia coli BL21