› 3l06

X-ray diffraction
2.81Å resolution

Crystal structure of N-acetyl-L-ornithine transcarbamylase E92V mutant complexed with carbamyl phosphate and N-succinyl-L-norvaline

Released:
DOI: 10.2210/pdb3l06/pdb
PDB entry 3l06 coloured by chain, front view.
PDB entry 3l06 coloured by chain, side view.
PDB entry 3l06 coloured by chain, top view.
Source organism: Xanthomonas campestris pv. campestris str. ATCC 33913
Primary publication:
A single mutation in the active site swaps the substrate specificity of N-acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine transcarbamylase.
Shi D, Yu X, Cabrera-Luque J, Chen TY, Roth L, Morizono H, Allewell NM, Tuchman M
Protein Sci 16 1689-99 (2007)
PMID: 17600144

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: 40.1 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

3 bound ligands:
Ligand SN0 1 x SN0
Ligand CP 1 x CP
Ligand SO4 1 x SO4
1 modified residue:
Ligand KCX 1 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: I213
Unit cell:
a: 129.721Å b: 129.721Å c: 129.721Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.256
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Structures and folding pathways of topologically knotted proteins.
Virnau et al. (2011)
4 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