› 5vwo

X-ray diffraction
1.77Å resolution

Ornithine aminotransferase inactivated by (1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP)

Released:
DOI: 10.2210/pdb5vwo/pdb
PDB entry 5vwo coloured by chain, front view.
PDB entry 5vwo coloured by chain, side view.
PDB entry 5vwo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover.
Mascarenhas R, Le HV, Clevenger KD, Lehrer HJ, Ringe D, Kelleher NL, Silverman RB, Liu D
Biochemistry 56 4951-4961 (2017)
PMID: 28816437

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:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137492 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ornithine aminotransferase, mitochondrial Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 404 amino acids
Theoretical weight: 44.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04181 (Residues: 36-439; Coverage: 92%)
Gene name: OAT
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 9QJ 3 x 9QJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P3221
Unit cell:
a: 115.305Å b: 115.305Å c: 187.991Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.178 0.21
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Design and Mechanism of GABA Aminotransferase Inactivators. Treatments for Epilepsies and Addictions.
Silverman RB. (2018)
9 other articles

2 mentions without citation

Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover.
Mascarenhas et al. (2017)
1 more