› 7t9z

X-ray diffraction
2.15Å resolution

Human Ornithine Aminotransferase (hOAT) crystallized at pH 6.0

Released:
DOI: 10.2210/pdb7t9z/pdb
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Source organism: Homo sapiens
Primary publication:
Determination of the pH dependence, substrate specificity, and turnovers of alternative substrates for human ornithine aminotransferase.
Butrin A, Butrin A, Wawrzak Z, Moran GR, Liu D
OpenAccess logo J Biol Chem 298 101969 (2022)
PMID: 35460691

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137490 (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

Ligands and Environments


Cofactor: Ligand PLP 3 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: C2
Unit cell:
a: 200.91Å b: 110.86Å c: 56.93Å
α: 90° β: 106.404° γ: 90°
R-values:
R R work R free
0.271 0.266 0.276
Expression system: Escherichia coli

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Citations

2 citation in other articles

Ornithine aminotransferase and carbamoyl phosphate synthetase 1 involved in ammonia metabolism serve as novel targets for early stages of gastric cancer.
Jiang et al. (2022)
1 more

1 mention without citation

Determination of the pH dependence, substrate specificity, and turnovers of alternative substrates for human ornithine aminotransferase.
Butrin et al. (2022)

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