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TitleStructural and Mechanistic Basis for the Inactivation of Human Ornithine Aminotransferase by (3 S ,4 S )-3-Amino-4-fluorocyclopentenecarboxylic Acid.
Journal, issue, pagesMolecules, Vol. 28, Year 2023
Publish dateOct 30, 2022 (structure data deposition date)
AuthorsShen, S. / Butrin, A. / Beaupre, B.A. / Ferreira, G.M. / Doubleday, P.F. / Grass, D.H. / Zhu, W. / Kelleher, N.L. / Moran, G.R. / Liu, D. / Silverman, R.B.
External linksMolecules / PubMed:36770800
MethodsX-ray diffraction
Resolution1.91 Å
Structure data

PDB-8ez1:
Human Ornithine Aminotransferase (hOAT) co-crystallized with its inactivator 3-Amino-4-fluorocyclopentenecarboxylic Acid
Method: X-RAY DIFFRACTION / Resolution: 1.91 Å

Chemicals

ChemComp-X8B:
(3E,4E)-4-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-3-iminocyclopent-1-ene-1-carboxylic acid

ChemComp-X8H:
(1R,3S,4Z)-3-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-4-iminocyclopentane-1-carboxylic acid

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / hOAT / OAT / inactivator / 3-Amino-4-fluorocyclopentenecarboxylic Acid / covalent modification

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