› 3kzc

X-ray diffraction
2.2Å resolution

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + N(2)-acetyl-L-ornithine = phosphate + N-acetyl-L-citrulline
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185718 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylornithine carbamoyltransferase Chain: A
Molecule details ›
Chain: A
Length: 359 amino acids
Theoretical weight: 40.13 KDa
Source organism: Xanthomonas campestris pv. campestris str. ATCC 33913
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8P8J2 (Residues: 1-339; Coverage: 100%)
Gene names: XCC2249, argF'
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: I213
Unit cell:
a: 128.039Å b: 128.039Å c: 128.039Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 0.276
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Pathways and regulation of bacterial arginine metabolism and perspectives for obtaining arginine overproducing strains.
Lu et al. (2006)
7 more

2 mentions without citation

Filling out the structural map of the NTF2-like superfamily.
Eberhardt et al. (2013)
1 more