X-ray diffraction
2.15Å resolution

Structure of ornithine aminotransferase triple mutant Y85I Y55A G320F

Source organism: Homo sapiens
Primary publication:
Determinants of substrate specificity in omega-aminotransferases.
J. Biol. Chem. 280 36409-16 (2005)
PMID: 16096275

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Ornithine aminotransferase, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 439 amino acids
Theoretical weight: 48.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P04181 (Residues: 1-439; Coverage: 100%)
  • Best match: P04181-2 (Residues: 1-301)
Gene name: OAT
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

Cofactor: Ligand PLP 3 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3221
Unit cell:
a: 115.95Å b: 115.95Å c: 188.343Å
α: 90° β: 90° γ: 120°
R R work R free
0.161 0.159 0.191
Expression system: Escherichia coli