2v5z
From Proteopedia
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| ==About this Structure== | ==About this Structure== | ||
| - | 2V5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=SAG:'>SAG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(flavin-containing) Amine oxidase (flavin-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] Known structural/functional Sites: <scene name='pdbsite=AC1:Fad Binding Site For Chain A'>AC1</scene>, <scene name='pdbsite=AC2:Sag Binding Site For Chain A'>AC2</scene>, <scene name='pdbsite=AC3:Fad Binding Site For Chain B'>AC3</scene> and <scene name='pdbsite=AC4:Sag Binding Site For Chain B'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5Z OCA].  | + | 2V5Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=SAG:'>SAG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Amine_oxidase_(flavin-containing) Amine oxidase (flavin-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] Known structural/functional Sites: <scene name='pdbsite=AC1:Fad+Binding+Site+For+Chain+A'>AC1</scene>, <scene name='pdbsite=AC2:Sag+Binding+Site+For+Chain+A'>AC2</scene>, <scene name='pdbsite=AC3:Fad+Binding+Site+For+Chain+B'>AC3</scene> and <scene name='pdbsite=AC4:Sag+Binding+Site+For+Chain+B'>AC4</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5Z OCA].  | 
| ==Reference== | ==Reference== | ||
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| [[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on  | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 10:49:57 2008'' | 
Revision as of 08:49, 3 February 2008
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STRUCTURE OF HUMAN MAO B IN COMPLEX WITH THE SELECTIVE INHIBITOR SAFINAMIDE
Overview
Structures of human monoamine oxidase B (MAO B) in complex with safinamide, and two coumarin derivatives, all sharing a common benzyloxy substituent, were determined by X-ray crystallography. These compounds competitively, inhibit MAO B with Ki values in the 0.1-0.5 muM range that are 30-700-fold, lower than those observed with MAO A. The inhibitors bind noncovalently to, MAO B, occupying both the entrance and the substrate cavities and showing, a similarly oriented benzyloxy substituent.
About this Structure
2V5Z is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Amine oxidase (flavin-containing), with EC number 1.4.3.4 Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
Structures of Human Monoamine Oxidase B Complexes with Selective Noncovalent Inhibitors: Safinamide and Coumarin Analogs., Binda C, Wang J, Pisani L, Caccia C, Carotti A, Salvati P, Edmondson DE, Mattevi A, J Med Chem. 2007 Oct 4;. PMID:17915852
Page seeded by OCA on Sun Feb 3 10:49:57 2008
Categories: Amine oxidase (flavin-containing) | Homo sapiens | Single protein | Binda, C. | Caccia, C. | Carotti, A. | Edmondson, D.E. | Mattevi, A. | Pisani, L. | Salvati, P. | Wang, J. | FAD | SAG | Fad | Flavoprotein | Human mao b structure | Membrane | Mitochondrion | Neuroprotection | Oxidoreductase | Parkinson's disease | Reversible inhibitor binding | Safinamide | Transmembrane
