3a7e

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Current revision (14:14, 1 November 2023) (edit) (undo)
 
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<StructureSection load='3a7e' size='340' side='right'caption='[[3a7e]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3a7e' size='340' side='right'caption='[[3a7e]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3a7e]] is a 1 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=3A7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A7E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3a7e]] is a 1 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=3A7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3A7E 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=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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]] 2.8&#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;'>[[3a7d|3a7d]], [[3bwm|3bwm]], [[3bwy|3bwy]], [[1vid|1vid]]</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=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">COMT ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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/Catechol_O-methyltransferase Catechol O-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.6 2.1.1.6] </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=3a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7e OCA], [https://pdbe.org/3a7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a7e RCSB], [https://www.ebi.ac.uk/pdbsum/3a7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7e 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=3a7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a7e OCA], [https://pdbe.org/3a7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3a7e RCSB], [https://www.ebi.ac.uk/pdbsum/3a7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3a7e ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/COMT_HUMAN COMT_HUMAN]] Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
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[https://www.uniprot.org/uniprot/COMT_HUMAN COMT_HUMAN] Catalyzes the O-methylation, and thereby the inactivation, of catecholamine neurotransmitters and catechol hormones. Also shortens the biological half-lives of certain neuroactive drugs, like L-DOPA, alpha-methyl DOPA and isoproterenol.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Catechol O-methyltransferase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Tsuji, E]]
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[[Category: Tsuji E]]
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[[Category: Alternative initiation]]
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[[Category: Catecholamine metabolism]]
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[[Category: Cell membrane]]
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[[Category: Comt]]
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[[Category: Magnesium]]
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[[Category: Membrane]]
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[[Category: Metal-binding]]
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[[Category: Methyltransferase]]
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[[Category: Neurotransmitter degradation]]
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[[Category: Phosphoprotein]]
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[[Category: S-adenosyl-l-methionine]]
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[[Category: Signal-anchor]]
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[[Category: Transferase]]
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[[Category: Transmembrane]]
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Current revision

Crystal structure of human COMT complexed with SAM and 3,5-dinitrocatechol

PDB ID 3a7e

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