1W4N

AGAO covalent complex with Tranylcypromine

Summary for 1W4N

• Entry DOI: 10.2210/pdb1w4n/pdb
• Related: 1AV4 1AVK 1AVL 1IQX 1IQY 1IU7 1IVU 1IVV 1IVW 1IVX 1RJO 1SIH 1SII 1UI7 1UI8 1W5Z 1W6C 1W6G 1WMN 1WMO 1WMP 2BT3
• Descriptor: PHENYLETHYLAMINE OXIDASE, COPPER (II) ION, SODIUM ION, ... (6 entities in total)
• Functional Keywords: amine oxidase, arthrobacter globiformis, copper containing, metal-binding, oxidoreductase, tcq, quinone, inhibited, tcp, tranylcypromine
• Biological source: ARTHROBACTER GLOBIFORMIS
• Total number of polymer chains: 2
• Total formula weight: 144953.95

Authors

Duff, A.P.,Trambaiolo, D.M.,Langley, D.B.,Juda, G.A.,Shepard, E.M.,Dooley, D.M.,Freeman, H.C.,Guss, J.M. (deposition date: 2004-07-27, release date: 2005-12-08, Last modification date: 2024-11-06)

Primary citation

Langley, D.B.,Trambaiolo, D.M.,Duff, A.P.,Dooley, D.M.,Freeman, H.C.,Guss, J.M.
Complexes of the Copper-Containing Amine Oxidase from Arthrobacter Globiformis with the Inhibitors Benzylhydrazine and Tranylcypromine.
Acta Crystallogr.,Sect.F, 64:577-, 2008

PubMed Abstract: Complexes of Arthrobacter globiformis amine oxidase (AGAO) with the inhibitors benzylhydrazine and tranylcypromine (an antidepressant drug) have been refined at 1.86 and 1.65 A resolution, respectively. Both inhibitors form covalent adducts with the TPQ cofactor. A tyrosine residue, proposed to act as a gate to the AGAO active site, is in its open conformation.

PubMed: 18607080
DOI: 10.1107/S174430910801556X

Experimental method

X-RAY DIFFRACTION (1.65 Å)