3a7e

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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==
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<StructureSection load='3a7e' size='340' side='right' caption='[[3a7e]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<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 [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>
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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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</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>
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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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<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>
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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='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>
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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'>[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>
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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'>[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>
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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>
</table>
</table>
== Function ==
== Function ==
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[[http://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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==See Also==
==See Also==
*[[Catechol O-methyltransferase|Catechol O-methyltransferase]]
*[[Catechol O-methyltransferase|Catechol O-methyltransferase]]
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*[[Catechol O-methyltransferase 3D structures|Catechol O-methyltransferase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Catechol O-methyltransferase]]
[[Category: Catechol O-methyltransferase]]
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Tsuji, E]]
[[Category: Tsuji, E]]
[[Category: Alternative initiation]]
[[Category: Alternative initiation]]

Revision as of 16:19, 22 December 2021

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

PDB ID 3a7e

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