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1W5Z

AGAO covalent complex with Benzylhydrazine

Summary for 1W5Z
Entry DOI10.2210/pdb1w5z/pdb
Related1W6C 1W6G
DescriptorPHENYLETHYLAMINE OXIDASE, COPPER (II) ION, SODIUM ION, ... (6 entities in total)
Functional Keywordsamine oxidase, arthrobacter globiformis, copper containing, metal-binding, oxidoreductase, tpq, quinone, inhibited, bh, benzylhydrazine, 3ty
Biological sourceARTHROBACTER GLOBIFORMIS
Total number of polymer chains1
Total formula weight72703.12
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: 2004-08-11, release date: 2005-12-08, Last modification date: 2023-12-13)
Primary citationLangley, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.86 Å)
Structure validation

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