2v5z

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<StructureSection load='2v5z' size='340' side='right'caption='[[2v5z]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='2v5z' size='340' side='right'caption='[[2v5z]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2v5z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2v5z]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2V5Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2V5Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SAG:(S)-(+)-2-[4-(FLUOROBENZYLOXY-BENZYLAMINO)PROPIONAMIDE]'>SAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gos|1gos]], [[1h8r|1h8r]], [[1oj9|1oj9]], [[1oja|1oja]], [[1ojb|1ojb]], [[1ojc|1ojc]], [[1ojd|1ojd]], [[1s2q|1s2q]], [[1s2y|1s2y]], [[1s3b|1s3b]], [[1s3e|1s3e]], [[2bk3|2bk3]], [[2bk4|2bk4]], [[2bk5|2bk5]], [[2byb|2byb]], [[2c64|2c64]], [[2c65|2c65]], [[2c66|2c66]], [[2c67|2c67]], [[2c70|2c70]], [[2c72|2c72]], [[2c73|2c73]], [[2c75|2c75]], [[2c76|2c76]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SAG:(S)-(+)-2-[4-(FLUOROBENZYLOXY-BENZYLAMINO)PROPIONAMIDE]'>SAG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5z OCA], [https://pdbe.org/2v5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v5z RCSB], [https://www.ebi.ac.uk/pdbsum/2v5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5z ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2v5z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2v5z OCA], [https://pdbe.org/2v5z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2v5z RCSB], [https://www.ebi.ac.uk/pdbsum/2v5z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2v5z ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AOFB_HUMAN 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2v5z ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2v5z ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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 microM 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.
 
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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 Nov 15;50(23):5848-52. Epub 2007 Oct 4. PMID:17915852<ref>PMID:17915852</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2v5z" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Monoamine oxidase|Monoamine oxidase]]
*[[Monoamine oxidase|Monoamine oxidase]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Monoamine oxidase]]
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[[Category: Binda C]]
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[[Category: Binda, C]]
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[[Category: Caccia C]]
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[[Category: Caccia, C]]
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[[Category: Carotti A]]
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[[Category: Carotti, A]]
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[[Category: Edmondson DE]]
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[[Category: Edmondson, D E]]
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[[Category: Mattevi A]]
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[[Category: Mattevi, A]]
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[[Category: Pisani L]]
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[[Category: Pisani, L]]
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[[Category: Salvati P]]
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[[Category: Salvati, P]]
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[[Category: Wang J]]
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[[Category: Wang, J]]
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[[Category: Fad]]
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[[Category: Flavoprotein]]
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[[Category: Human mao b structure]]
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[[Category: Membrane]]
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[[Category: Mitochondrion]]
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[[Category: Neuroprotection]]
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[[Category: Oxidoreductase]]
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[[Category: Parkinson's disease]]
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[[Category: Reversible inhibitor binding]]
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[[Category: Safinamide]]
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[[Category: Transmembrane]]
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Current revision

Structure of human MAO B in complex with the selective inhibitor safinamide

PDB ID 2v5z

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