5eqc

X-ray diffraction
2.2Å resolution

Structure of the ornithine aminotransferase from Toxoplasma gondii crystallized in presence of oxidized glutathione reveals partial occupancy of PLP at the protein active site

Released:
Source organism: Toxoplasma gondii
Entry authors: Filippova EV, Minasov G, Flores K, Le HV, Silverman RB, McLeod RL, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

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-197464 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine aminotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 441 amino acids
Theoretical weight: 48.39 KDa
Source organism: Toxoplasma gondii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: S8EY38 (Residues: 1-441; Coverage: 100%)
Gene name: TGME49_269110
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P43
Unit cell:
a: 109.406Å b: 109.406Å c: 109.883Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.146 0.145 0.181
Expression system: Escherichia coli BL21(DE3)