› 2oat

X-ray diffraction
1.95Å resolution

ORNITHINE AMINOTRANSFERASE COMPLEXED WITH 5-FLUOROMETHYLORNITHINE

Released:
DOI: 10.2210/pdb2oat/pdb
PDB entry 2oat coloured by chain, front view.
PDB entry 2oat coloured by chain, side view.
PDB entry 2oat coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human ornithine aminotransferase complexed with the highly specific and potent inhibitor 5-fluoromethylornithine.
Storici P, Capitani G, Müller R, Schirmer T, Jansonius JN
J Mol Biol 285 297-309 (1999)
PMID: 9878407

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

Assemblies composition:
homo tetramer
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: 48.59 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:
Ligand PFM 3 x PFM
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

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Citations

5 review citations

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Eliot et al. (2004)
4 more

12 mentions without citation

Ornithine aminotransferase versus GABA aminotransferase: implications for the design of new anticancer drugs.
Lee et al. (2015)
11 more