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3a7e
From Proteopedia
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==Crystal structure of human COMT complexed with SAM and 3,5-dinitrocatechol== | ==Crystal structure of human COMT complexed with SAM and 3,5-dinitrocatechol== | ||
<StructureSection load='3a7e' size='340' side='right' caption='[[3a7e]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3a7e' size='340' side='right' caption='[[3a7e]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3a7e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3a7e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A7E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A7E FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a7d|3a7d]], [[3bwm|3bwm]], [[3bwy|3bwy]], [[1vid|1vid]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3a7d|3a7d]], [[3bwm|3bwm]], [[3bwy|3bwy]], [[1vid|1vid]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COMT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] </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=3a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7e OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a7e RCSB], [http://www.ebi.ac.uk/pdbsum/3a7e PDBsum]</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=3a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7e OCA], [http://pdbe.org/3a7e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3a7e RCSB], [http://www.ebi.ac.uk/pdbsum/3a7e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7e ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=3a7e ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Catechol O-methyltransferase]] | [[Category: Catechol O-methyltransferase]] | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Tsuji, E]] | [[Category: Tsuji, E]] | ||
[[Category: Alternative initiation]] | [[Category: Alternative initiation]] | ||
Revision as of 15:36, 5 August 2016
Crystal structure of human COMT complexed with SAM and 3,5-dinitrocatechol
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Categories: Catechol O-methyltransferase | Human | Tsuji, E | Alternative initiation | Catecholamine metabolism | Cell membrane | Comt | Magnesium | Membrane | Metal-binding | Methyltransferase | Neurotransmitter degradation | Phosphoprotein | S-adenosyl-l-methionine | Signal-anchor | Transferase | Transmembrane
