› 3pnu

X-ray diffraction
2.4Å resolution

2.4 Angstrom Crystal Structure of Dihydroorotase (pyrC) from Campylobacter jejuni.

Released:
DOI: 10.2210/pdb3pnu/pdb
PDB entry 3pnu coloured by chain, front view.
PDB entry 3pnu coloured by chain, side view.
PDB entry 3pnu coloured by chain, top view.
Source organism: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171058 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotase Chains: A, B
Molecule details ›
Chains: A, B
Length: 359 amino acids
Theoretical weight: 41.26 KDa
Source organism: Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0PBP6 (Residues: 1-335; Coverage: 100%)
Gene names: Cj0259, pyrC
Sequence domains: Amidohydrolase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand PO4 2 x PO4
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 69.52Å b: 80.802Å c: 154.878Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.25
Expression system: Escherichia coli

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