› 4f2g

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo hexamer
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-173995 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine carbamoyltransferase Chain: A
Molecule details ›
Chain: A
Length: 309 amino acids
Theoretical weight: 35.46 KDa
Source organism: Burkholderia thailandensis E264
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2T0L1 (Residues: 1-309; Coverage: 100%)
Gene names: BTH_I0732, argF, argF-1
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

2 bound ligands:
Ligand EDO 1 x EDO
Ligand PO4 7 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P4132
Unit cell:
a: 141.25Å b: 141.25Å c: 141.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.196
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.
Dailey et al. (2017)
10 more

2 mentions without citation

Combining functional and structural genomics to sample the essential Burkholderia structome.
Baugh et al. (2013)
1 more