3zyx: Difference between revisions

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-==CRYSTAL STRUCTURE OF HUMAN MONOAMINE OXIDASE B IN COMPLEX WITH METHYLENE BLUE AND BEARING THE DOUBLE MUTATION I199A-Y326A==
-<StructureSection load='3zyx' size='340' side='right' caption='[[3zyx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+==Crystal structure of human monoamine oxidase B in complex with methylene blue and bearing the double mutation I199A-Y326A==
+<StructureSection load='3zyx' size='340' side='right'caption='[[3zyx]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3zyx]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZYX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZYX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3zyx]] 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=3ZYX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZYX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MBT:3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM'>MBT</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c67|2c67]], [[1s3e|1s3e]], [[2c73|2c73]], [[2v60|2v60]], [[1oj9|1oj9]], [[2vz2|2vz2]], [[1ojd|1ojd]], [[1s3b|1s3b]], [[2c66|2c66]], [[2xfo|2xfo]], [[2bk5|2bk5]], [[1h8r|1h8r]], [[2c70|2c70]], [[2xfn|2xfn]], [[2bk3|2bk3]], [[2c76|2c76]], [[2vrl|2vrl]], [[1oja|1oja]], [[2v5z|2v5z]], [[2xfu|2xfu]], [[2byb|2byb]], [[2vrm|2vrm]], [[2c65|2c65]], [[2c64|2c64]], [[2xcg|2xcg]], [[2xfp|2xfp]], [[2bk4|2bk4]], [[2c75|2c75]], [[2v61|2v61]], [[1s2y|1s2y]], [[2c72|2c72]], [[1gos|1gos]], [[1s2q|1s2q]], [[2xfq|2xfq]], [[1ojc|1ojc]]</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=MBT:3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM'>MBT</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Monoamine_oxidase Monoamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.4 1.4.3.4] </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=3zyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyx OCA], [https://pdbe.org/3zyx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zyx RCSB], [https://www.ebi.ac.uk/pdbsum/3zyx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zyx ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3zyx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zyx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zyx RCSB], [http://www.ebi.ac.uk/pdbsum/3zyx PDBsum]</span></td></tr>
 </table>
+== Function ==
+[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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 16: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3zyx" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 24: / Line 27: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Monoamine oxidase]]
+[[Category: Large Structures]]
-[[Category: Binda, C]]
+[[Category: Binda C]]
-[[Category: Edmondson, D E]]
+[[Category: Edmondson DE]]
-[[Category: Mattevi, A]]
+[[Category: Mattevi A]]
-[[Category: Milczek, E M]]
+[[Category: Milczek EM]]
-[[Category: Rovida, S]]
+[[Category: Rovida S]]
-[[Category: Inhibitor]]
-[[Category: Oxidoreductase]]