› 2byj

X-ray diffraction
3.02Å resolution

Ornithine aminotransferase mutant Y85I

Released:
DOI: 10.2210/pdb2byj/pdb
PDB entry 2byj coloured by chain, front view.
PDB entry 2byj coloured by chain, side view.
PDB entry 2byj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Determinants of substrate specificity in omega-aminotransferases.
Markova M, Peneff C, Hewlins MJ, Schirmer T, John RA
J Biol Chem 280 36409-16 (2005)
PMID: 16096275

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137491 (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

Quick links

Citations

4 review citations

Structural biology of proline catabolism.
Tanner JJ. (2008)
3 more