2eh6

X-ray diffraction
1.9Å resolution

Crystal structure of acetylornithine aminotransferase from Aquifex aeolicus VF5

Released:
Source organism: Aquifex aeolicus VF5
Entry authors: Mizutani H, Kunishima N, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate 5-semialdehyde + L-glutamate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-130306 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylornithine aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 375 amino acids
Theoretical weight: 41.94 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O66442 (Residues: 2-376; Coverage: 100%)
Gene names: aq_023, argD
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: I222
Unit cell:
a: 101.094Å b: 124.7Å c: 131.614Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.198 0.221
Expression system: Escherichia coli