1LVN

CRYSTAL STRUCTURE OF E. COLI AMINE OXIDASE COMPLEXED WITH TRANYLCYPROMINE

Summary for 1LVN

• Entry DOI: 10.2210/pdb1lvn/pdb
• Related: 1D6U 1D6Y 1D6Z 1DYU 1OAC 1SPU
• Descriptor: Copper amine oxidase, COPPER (II) ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: inhibitor complex, oxidoreductase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P46883
• Total number of polymer chains: 2
• Total formula weight: 163255.25

Authors

Wilmot, C.M.,Phillips, S.E. (deposition date: 2002-05-28, release date: 2003-08-05, Last modification date: 2023-11-15)

Primary citation

Wilmot, C.M.,Saysell, C.G.,Blessington, A.,Conn, D.A.,Kurtis, C.R.,McPherson, M.J.,Knowles, P.F.,Phillips, S.E.
Medical implications from the crystal structure of a copper-containing amine oxidase complexed with the antidepressant drug tranylcypromine.
Febs Lett., 576:301-305, 2004

PubMed Abstract: The X-ray crystal structure of the copper-containing quinoprotein amine oxidase from E. coli has been determined in complex with the antidepressant drug tranylcypromine to 2.4 A resolution. The drug is a racemic mix of two enantiomers, but only one is seen bound to the enzyme. The other enantiomer is not acting as a substrate for the enzyme as no catalytic activity was detected when the enzyme was initially exposed to the drug. The inhibition of human copper amine oxidases could be a source of side-effects in its use as an antidepressant to inhibit the flavin-containing monoamine oxidases in the brain.

PubMed: 15498552
DOI: 10.1016/j.febslet.2004.09.031

Experimental method

X-RAY DIFFRACTION (2.4 Å)