› 2z26

X-ray diffraction
1.29Å resolution

Thr110Ala dihydroorotase from E. coli

Released:
DOI: 10.2210/pdb2z26/pdb
PDB entry 2z26 coloured by chain, front view.
PDB entry 2z26 coloured by chain, side view.
PDB entry 2z26 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Kinetic and structural analysis of mutant Escherichia coli dihydroorotases: a flexible loop stabilizes the transition state.
Lee M, Maher MJ, Christopherson RI, Guss JM
Biochemistry 46 10538-50 (2007)
PMID: 17711307

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-138326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotase Chains: A, B
Molecule details ›
Chains: A, B
Length: 347 amino acids
Theoretical weight: 38.74 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

4 bound ligands:
Ligand ZN 4 x ZN
Ligand DOR 2 x DOR
Ligand MLI 1 x MLI
Ligand NCD 1 x NCD
1 modified residue:
Ligand KCX 2 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 51.493Å b: 78.885Å c: 180.091Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.131 0.129 0.154
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

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

3 mentions without citation

Crystal structures of vertebrate dihydropyrimidinase and complexes from Tetraodon nigroviridis with lysine carbamylation: metal and structural requirements for post-translational modification and function.
Hsieh et al. (2013)
2 more