X-ray diffraction
1.8Å resolution

Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with N-acetyl-L-ornirthine


Function and Biology Details

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
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)
  • Canonical: Q8P8J2 (Residues: 1-339; Coverage: 100%)
Gene names: XCC2249, argF'
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: I213
Unit cell:
a: 130.198Å b: 130.198Å c: 130.198Å
α: 90° β: 90° γ: 90°
R R work R free
0.189 0.189 0.212
Expression system: Escherichia coli BL21(DE3)