5viu

X-ray diffraction
1.65Å resolution

Crystal Structure of Acetylornithine Aminotransferase from Elizabethkingia anophelis

Released:
Source organism: Elizabethkingia anophelis
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Reaction catalysed:
L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino acid
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-100502 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ornithine aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 419 amino acids
Theoretical weight: 46.1 KDa
Source organism: Elizabethkingia anophelis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A077E919 (Residues: 1-411; Coverage: 100%)
Gene name: BD94_0267
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2
Unit cell:
a: 136.6Å b: 77.47Å c: 104.96Å
α: 90° β: 129.46° γ: 90°
R-values:
R R work R free
0.156 0.155 0.18
Expression system: Escherichia coli BL21(DE3)