2xfq: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(4 intermediate revisions by the same user not shown)
Line 1: Line 1:


==rasagiline-inhibited human monoamine oxidase B in complex with 2-(2- benzofuranyl)-2-imidazoline==
==Rasagiline-inhibited human monoamine oxidase B in complex with 2-(2- benzofuranyl)-2-imidazoline==
<StructureSection load='2xfq' size='340' side='right' caption='[[2xfq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2xfq' size='340' side='right'caption='[[2xfq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2xfq]] 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=2XFQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XFQ FirstGlance]. <br>
<table><tr><td colspan='2'>[[2xfq]] 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=2XFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XFQ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C15:N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE'>C15</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=RAS:(1R)-N-(PROP-2-EN-1-YL)-2,3-DIHYDRO-1H-INDEN-1-AMINE'>RAS</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</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]], [[1oja|1oja]], [[2v5z|2v5z]], [[1s3e|1s3e]], [[2c73|2c73]], [[1ojb|1ojb]], [[2v60|2v60]], [[2byb|2byb]], [[2vrm|2vrm]], [[2c65|2c65]], [[2c64|2c64]], [[2xcg|2xcg]], [[1oj9|1oj9]], [[1ojd|1ojd]], [[2vz2|2vz2]], [[1s3b|1s3b]], [[2c66|2c66]], [[2bk4|2bk4]], [[2bk5|2bk5]], [[1h8r|1h8r]], [[2c70|2c70]], [[2c75|2c75]], [[2bk3|2bk3]], [[2v61|2v61]], [[2c72|2c72]], [[1s2y|1s2y]], [[1gos|1gos]], [[1s2q|1s2q]], [[2c76|2c76]], [[2vrl|2vrl]], [[1ojc|1ojc]], [[2xfo|2xfo]], [[2xfn|2xfn]], [[2xfp|2xfp]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C15:N-DODECYL-N,N-DIMETHYL-3-AMMONIO-1-PROPANESULFONATE'>C15</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=RAS:(1R)-N-(PROP-2-EN-1-YL)-2,3-DIHYDRO-1H-INDEN-1-AMINE'>RAS</scene>, <scene name='pdbligand=XCG:2-(2-BENZOFURANYL)-2-IMIDAZOLINE'>XCG</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=2xfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfq OCA], [https://pdbe.org/2xfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xfq RCSB], [https://www.ebi.ac.uk/pdbsum/2xfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfq 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=2xfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xfq OCA], [http://pdbe.org/2xfq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xfq RCSB], [http://www.ebi.ac.uk/pdbsum/2xfq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xfq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[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]]
Line 16: Line 15:
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/2xfq_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xf/2xfq_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
Line 30: Line 29:
</div>
</div>
<div class="pdbe-citations 2xfq" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 2xfq" style="background-color:#fffaf0;"></div>
==See Also==
*[[Monoamine oxidase|Monoamine oxidase]]
== References ==
== References ==
<references/>
<references/>
Line 35: Line 37:
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Monoamine oxidase]]
[[Category: Large Structures]]
[[Category: Binda, C]]
[[Category: Binda C]]
[[Category: Bonivento, D]]
[[Category: Bonivento D]]
[[Category: Edmondson, D E]]
[[Category: Edmondson DE]]
[[Category: Holt, A]]
[[Category: Holt A]]
[[Category: Mattevi, A]]
[[Category: Mattevi A]]
[[Category: McDonald, G R]]
[[Category: McDonald GR]]
[[Category: Milczek, E M]]
[[Category: Milczek EM]]
[[Category: Flavoprotein]]
[[Category: Oxidoreductase]]