› 3kzo

X-ray diffraction
1.9Å resolution

Crystal structure of N-acetyl-L-ornithine transcarbamylase complexed with carbamyl phosphate and N-acetyl-L-norvaline

Released:
DOI: 10.2210/pdb3kzo/pdb
PDB entry 3kzo coloured by chain, front view.
PDB entry 3kzo coloured by chain, side view.
PDB entry 3kzo coloured by chain, top view.
Source organism: Xanthomonas campestris pv. campestris str. ATCC 33913
Primary publication:
Structures of N-acetylornithine transcarbamoylase from Xanthomonas campestris complexed with substrates and substrate analogs imply mechanisms for substrate binding and catalysis.
Shi D, Yu X, Roth L, Morizono H, Tuchman M, Allewell NM
Proteins 64 532-42 (2006)
PMID: 16741992

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

4 bound ligands:
Ligand AN0 1 x AN0
Ligand CP 1 x CP
Ligand GOL 1 x GOL
Ligand SO4 1 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: 129.953Å b: 129.953Å c: 129.953Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Surprising arginine biosynthesis: a reappraisal of the enzymology and evolution of the pathway in microorganisms.
Xu et al. (2007)
2 more

3 mentions without citation

Coupling Protein Side-Chain and Backbone Flexibility Improves the Re-design of Protein-Ligand Specificity.
Ollikainen et al. (2015)
2 more