3po7

Human monoamine oxidase B in complex with zonisamide

spinqualitylabelsall models 3po7, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3po7 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: FAD, ZON Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function AOFB_HUMAN Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine. Publication Abstract from PubMed The binding of zonisamide to purified, recombinant monoamine oxidases (MAOs) has been investigated. It is a competitive inhibitor of human MAO B (K(i) = 3.1 +/- 0.3 muM), of rat MAO B (K(i) = 2.9 +/- 0.5 muM), and of zebrafish MAO (K(i) = 30.8 +/- 5.3 muM). No inhibition is observed with purified human or rat MAO A. The 1.8 A structure of the MAO B complex demonstrates that it binds within the substrate cavity. Interactions of Monoamine Oxidases with the Antiepileptic Drug Zonisamide: Specificity of Inhibition and Structure of the Human Monoamine Oxidase B Complex.,Binda C, Aldeco M, Mattevi A, Edmondson DE J Med Chem. 2010 Dec 22. PMID:21175212 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Monoamine oxidase

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