2byj

X-ray diffraction
3.02Å resolution

Ornithine aminotransferase mutant Y85I

Released:
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
Macromolecule:
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
UniProt:
  • Canonical: P04181 (Residues: 1-439; Coverage: 100%)
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: RIGAKU
Spacegroup: P3221
Unit cell:
a: 115.723Å b: 115.723Å c: 186.551Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.207 0.226
Expression system: Escherichia coli