› 1j79

X-ray diffraction
1.7Å resolution

Molecular Structure of Dihydroorotase: A Paradigm for Catalysis Through the Use of a Binuclear Metal Center

Released:
DOI: 10.2210/pdb1j79/pdb
PDB entry 1j79 coloured by chain, front view.
PDB entry 1j79 coloured by chain, side view.
PDB entry 1j79 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center.
Thoden JB, Phillips GN, Neal TM, Raushel FM, Holden HM
Biochemistry 40 6989-97 (2001)
PMID: 11401542

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotase Chains: A, B
Molecule details ›
Chains: A, B
Length: 347 amino acids
Theoretical weight: 38.83 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P05020 (Residues: 2-348; Coverage: 100%)
Gene names: JW1049, b1062, pyrC
Sequence domains: Amidohydrolase family
Structure domains: Metal-dependent hydrolases

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand ORO 1 x ORO
Ligand NCD 2 x NCD
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 51.6Å b: 78.8Å c: 180.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.258
Expression system: Escherichia coli

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Citations

12 review citations

Mammalian pyrimidine biosynthesis: fresh insights into an ancient pathway.
Evans et al. (2004)
11 more

15 mentions without citation

Structural bases for CRMP function in plexin-dependent semaphorin3A signaling.
Deo et al. (2004)
14 more