PDBe 2oat

X-ray diffraction
1.95Å resolution

ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE

Released:

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

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine aminotransferase, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 439 amino acids
Theoretical weight: 48.59 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04181 (Residues: 1-439; Coverage: 100%)
Gene name: OAT
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P3221
Unit cell:
a: 115.28Å b: 115.28Å c: 186.81Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.204 0.232
Expression system: Escherichia coli