3bwy - Revision history

OCA at 12:17, 30 August 2023

OCA — Wed, 30 Aug 2023 12:17:42 GMT

←Older revision		Revision as of 12:17, 30 August 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3bwy]] 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=3BWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BWY FirstGlance]. <br>		<table><tr><td colspan='2'>[[3bwy]] 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=3BWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BWY FirstGlance]. <br>
-	</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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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]] 1.3Å</td></tr>
-	<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 Homo sapiens])</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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
-	<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>	+
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [https://pdbe.org/3bwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [https://www.ebi.ac.uk/pdbsum/3bwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bwy 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=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [https://pdbe.org/3bwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [https://www.ebi.ac.uk/pdbsum/3bwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bwy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[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.	+	[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>
-	[[Category: Catechol O-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Parson, W W]]~~	+	[[Category: Le Trong I]]
-	~~[[Category: Rutherford, K]]~~	+	[[Category: Parson WW]]
-	~~[[Category: Stenkamp, R E]]~~	+	[[Category: Rutherford K]]
-	~~[[Category:~~ Trong, I Le]]	+	[[Category: Stenkamp RE]]
-	[[Category: ~~Comt~~]]	+
-	[[Category: ~~Dnc~~]]	+
-	[[Category: ~~Methyltransferase]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Rossmann fold]]~~	+
-	~~[[Category: Sam]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 08:27, 19 January 2022

OCA — Wed, 19 Jan 2022 08:27:51 GMT

←Older revision		Revision as of 08:27, 19 January 2022
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	==Crystal Structure of Human 108M Catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol==		==Crystal Structure of Human 108M Catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol==
-	<StructureSection load='3bwy' size='340' side='right' caption='[[3bwy]], [[Resolution\|resolution]] 1.30Å' scene=''>	+	<StructureSection load='3bwy' size='340' side='right'caption='[[3bwy]], [[Resolution\|resolution]] 1.30Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3bwy]] is a 1 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=3BWY OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3BWY FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3bwy]] 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=3BWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BWY 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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</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" id="ligandDat"><scene name='pdbligand=DNC:3,5-DINITROCATECHOL'>DNC</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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 Homo sapiens])</td></tr>	+	<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 Homo sapiens])</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'>[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>
-	<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=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [~~http~~://pdbe.org/3bwy PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3bwy PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3bwy 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=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [https://pdbe.org/3bwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [https://www.ebi.ac.uk/pdbsum/3bwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bwy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~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.	+	[[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]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bw/3bwy_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bw/3bwy_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 3bwy" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3bwy" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Catechol O-methyltransferase 3D structures\|Catechol O-methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 36:		Line 39:
	[[Category: Catechol O-methyltransferase]]		[[Category: Catechol O-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
		+	[[Category: Large Structures]]
	[[Category: Parson, W W]]		[[Category: Parson, W W]]
	[[Category: Rutherford, K]]		[[Category: Rutherford, K]]

OCA at 08:13, 25 October 2017

OCA — Wed, 25 Oct 2017 08:13:21 GMT

←Older revision		Revision as of 08:13, 25 October 2017
Line 1:		Line 1:
		+
	==Crystal Structure of Human 108M Catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol==		==Crystal Structure of Human 108M Catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol==
	<StructureSection load='3bwy' size='340' side='right' caption='[[3bwy]], [[Resolution\|resolution]] 1.30Å' scene=''>		<StructureSection load='3bwy' size='340' side='right' caption='[[3bwy]], [[Resolution\|resolution]] 1.30Å' scene=''>
Line 6:		Line 7:
	<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 Homo sapiens])</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 Homo sapiens])</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=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [http://pdbe.org/3bwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [http://www.ebi.ac.uk/pdbsum/3bwy 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=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [http://pdbe.org/3bwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [http://www.ebi.ac.uk/pdbsum/3bwy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bwy ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	</div>		</div>
	<div class="pdbe-citations 3bwy" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3bwy" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Catechol O-methyltransferase\|Catechol O-methyltransferase]]
	== References ==		== References ==
	<references/>		<references/>
Line 45:		Line 43:
	[[Category: Dnc]]		[[Category: Dnc]]
	[[Category: Methyltransferase]]		[[Category: Methyltransferase]]
		+	[[Category: Polymorphism]]
	[[Category: Rossmann fold]]		[[Category: Rossmann fold]]
	[[Category: Sam]]		[[Category: Sam]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 08:23, 8 February 2016

OCA — Mon, 08 Feb 2016 08:23:07 GMT

←Older revision		Revision as of 08:23, 8 February 2016
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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 Homo sapiens])</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 Homo sapiens])</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=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [http://www.ebi.ac.uk/pdbsum/3bwy 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=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [http://pdbe.org/3bwy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [http://www.ebi.ac.uk/pdbsum/3bwy PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	<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/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</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=3bwy ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3bwy" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 21:56, 24 December 2014

OCA — Wed, 24 Dec 2014 21:56:27 GMT

←Older revision		Revision as of 21:56, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3bwy]] is a 1 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=3BWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BWY FirstGlance]. <br>		<table><tr><td colspan='2'>[[3bwy]] is a 1 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=3BWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BWY FirstGlance]. <br>
-	</td></tr><tr><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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene><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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
-	<tr><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 Homo sapiens])</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 Homo sapiens])</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [http://www.ebi.ac.uk/pdbsum/3bwy 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=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [http://www.ebi.ac.uk/pdbsum/3bwy PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[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.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 37:
	[[Category: Catechol O-methyltransferase]]		[[Category: Catechol O-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Parson, W W.]]	+	[[Category: Parson, W W]]
-	[[Category: Rutherford, K.]]	+	[[Category: Rutherford, K]]
-	[[Category: Stenkamp, R E.]]	+	[[Category: Stenkamp, R E]]
-	[[Category: Trong, I Le.]]	+	[[Category: Trong, I Le]]
	[[Category: Comt]]		[[Category: Comt]]
	[[Category: Dnc]]		[[Category: Dnc]]

OCA at 21:29, 2 October 2014

OCA — Thu, 02 Oct 2014 21:29:02 GMT

←Older revision		Revision as of 21:29, 2 October 2014
Line 1:		Line 1:
-	[[~~Image:~~3bwy.~~png~~\|~~left~~\|200px]]	+	==Crystal Structure of Human 108M Catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol==
		+	<StructureSection load='3bwy' size='340' side='right' caption='[[3bwy]], [[Resolution\|resolution]] 1.30Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3bwy]] is a 1 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=3BWY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3BWY FirstGlance]. <br>
		+	</td></tr><tr><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=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene><br>
		+	<tr><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 Homo sapiens])</td></tr>
		+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwy OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3bwy RCSB], [http://www.ebi.ac.uk/pdbsum/3bwy PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bw/3bwy_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</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/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Catechol O-methyltransferase (COMT) plays important roles in the metabolism of catecholamine neurotransmitters and catechol estrogens. The development of COMT inhibitors for use in the treatment of Parkinson's disease has been aided by crystallographic structures of the rat enzyme. However, the human and rat proteins have significantly different substrate specificities. Additionally, human COMT contains a common valine-methionine polymorphism at position 108. The methionine protein is less stable than the valine polymorph, resulting in decreased enzyme activity and protein levels in vivo. Here we describe the crystal structures of the 108V and 108M variants of the soluble form of human COMT bound with S-adenosylmethionine (SAM) and a substrate analog, 3,5-dinitrocatechol. The polymorphic residue 108 is located in the alpha5-beta3 loop, buried in a hydrophobic pocket approximately 16 A from the SAM-binding site. The 108V and 108M structures are very similar overall [RMSD of C(alpha) atoms between two structures (C(alpha) RMSD)=0.2 A], and the active-site residues are superposable, in accord with the observation that SAM stabilizes 108M COMT. However, the methionine side chain is packed more tightly within the polymorphic site and, consequently, interacts more closely with residues A22 (alpha2) and R78 (alpha4) than does valine. These interactions of the larger methionine result in a 0.7-A displacement in the backbone structure near residue 108, which propagates along alpha1 and alpha5 toward the SAM-binding site. Although the overall secondary structures of the human and rat proteins are very similar (C(alpha) RMSD=0.4 A), several nonconserved residues are present in the SAM-(I89M, I91M, C95Y) and catechol- (C173V, R201M, E202K) binding sites. The human protein also contains three additional solvent-exposed cysteine residues (C95, C173, C188) that may contribute to intermolecular disulfide bond formation and protein aggregation.

-	~~{{STRUCTURE_3bwy\| PDB=3bwy \| SCENE= }}~~	+	Crystal structures of human 108V and 108M catechol O-methyltransferase.,Rutherford K, Le Trong I, Stenkamp RE, Parson WW J Mol Biol. 2008 Jun 27;380(1):120-30. Epub 2008 Apr 23. PMID:18486144<ref>PMID:18486144</ref>

-	~~===Crystal Structure~~ of ~~Human 108M Catechol O-methyltransferase bound with~~ S~~-adenosylmethionine and inhibitor dinitrocatechol===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

-	~~{{ABSTRACT_PUBMED_18486144}}~~	+	==See Also==
-		+	*[[Catechol O-methyltransferase\|Catechol O-methyltransferase]]
-	==~~About this Structure~~==	+	== References ==
-	[[~~3bwy~~]] is a 1 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=3BWY OCA].	+	<references/>
-		+	__TOC__
-	==~~Reference~~==	+	</StructureSection>
-	<~~ref group="xtra">PMID:018486144<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Catechol O-methyltransferase]]		[[Category: Catechol O-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "3bwy" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 23:10:56 GMT

Protected "3bwy" [edit=sysop:move=sysop]

←Older revision

Revision as of 23:10, 7 January 2013

OCA at 23:10, 7 January 2013

OCA — Mon, 07 Jan 2013 23:10:53 GMT

←Older revision		Revision as of 23:10, 7 January 2013
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3bwy.png\|left\|200px]]		[[Image:3bwy.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3bwy", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3bwy\| PDB=3bwy \| SCENE= }}		{{STRUCTURE_3bwy\| PDB=3bwy \| SCENE= }}

	===Crystal Structure of Human 108M Catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol===		===Crystal Structure of Human 108M Catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18486144}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18486144 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_18486144}}		{{ABSTRACT_PUBMED_18486144}}
-
-	==Disease==
-	Known disease associated with this structure: Panic disorder, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=116790 116790]], Schizophrenia, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=116790 116790]]

	==About this Structure==		==About this Structure==
-	~~3BWY~~ is a 1 chain structure of 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=3BWY OCA].	+	[[3bwy]] is a 1 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=3BWY OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18486144~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018486144</ref><references group="xtra"/>
	[[Category: Catechol O-methyltransferase]]		[[Category: Catechol O-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 36:		Line 21:
	[[Category: Dnc]]		[[Category: Dnc]]
	[[Category: Methyltransferase]]		[[Category: Methyltransferase]]
-	[[Category: Polymorphism]]
	[[Category: Rossmann fold]]		[[Category: Rossmann fold]]
	[[Category: Sam]]		[[Category: Sam]]
-		+	[[Category: Transferase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Mon Feb 16 20:33:19 2009''~~	+

OCA at 18:33, 16 February 2009

OCA — Mon, 16 Feb 2009 18:33:20 GMT

←Older revision		Revision as of 18:33, 16 February 2009
Line 23:		Line 23:

	==About this Structure==		==About this Structure==
-	3BWY is a ~~[[Single protein]]~~ structure of 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=3BWY OCA].	+	3BWY is a 1 chain structure of 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=3BWY OCA].

	==Reference==		==Reference==
-	~~Crystal Structures of Human 108V and 108M Catechol O-Methyltransferase., Rutherford K, Le Trong I, Stenkamp RE, Parson WW, J Mol Biol. 2008 Apr 23;.~~ PMID:~~[http:~~//~~www.ncbi.nlm.nih.gov/pubmed/18486144 18486144]~~	+	<ref group="xtra">PMID:18486144</ref><references group="xtra"/>
	[[Category: Catechol O-methyltransferase]]		[[Category: Catechol O-methyltransferase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Single protein]]
	[[Category: Parson, W W.]]		[[Category: Parson, W W.]]
	[[Category: Rutherford, K.]]		[[Category: Rutherford, K.]]
Line 41:		Line 40:
	[[Category: Sam]]		[[Category: Sam]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon ~~Jul 28 00~~:44:~~39 2008~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 20:33:19 2009''

OCA at 21:44, 27 July 2008

OCA — Sun, 27 Jul 2008 21:44:42 GMT

←Older revision		Revision as of 21:44, 27 July 2008
Line 1:		Line 1:
-	[[Image:3bwy.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:3bwy.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_3bwy\| PDB=3bwy \| SCENE= }}		{{STRUCTURE_3bwy\| PDB=3bwy \| SCENE= }}

-	~~'''~~Crystal Structure of Human 108M Catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol~~'''~~	+	===Crystal Structure of Human 108M Catechol O-methyltransferase bound with S-adenosylmethionine and inhibitor dinitrocatechol===


-	~~==Overview==~~	+	<!--
-	~~Catechol O-methyltransferase (COMT) plays important roles in the metabolism of catecholamine neurotransmitters and catechol estrogens.~~ The ~~development of COMT inhibitors for use in the treatment of Parkinson's disease has been aided by crystallographic structures of the rat enzyme. However~~, ~~the human and rat proteins have significantly different substrate specificities. Additionally~~, ~~human COMT contains a common valine-methionine polymorphism at position 108. The methionine protein is less stable than~~ the ~~valine polymorph, resulting in decreased enzyme activity and protein levels in vivo. Here we describe~~ the ~~crystal structures of the 108V and 108M variants of the soluble form of human COMT bound with S-adenosylmethionine~~ (~~SAM) and a substrate analog, 3,5-dinitrocatechol~~. ~~The polymorphic residue 108 is located in the alpha5-beta3 loop, buried in a hydrophobic pocket approximately 16 A from the SAM-binding site~~. ~~The 108V and 108M structures are very similar overall [RMSD of C(alpha~~) ~~atoms between two structures (C(alpha) RMSD)=0.2 A]~~, ~~and the active-site residues are superposable, in accord with the observation that SAM stabilizes 108M COMT. However, the methionine side chain~~ is ~~packed more tightly within~~ the ~~polymorphic site and, consequently, interacts more closely with residues A22 (alpha2) and R78 (alpha4) than does valine~~. ~~These interactions of the larger methionine result in a 0.7~~-~~A displacement in the backbone structure near residue 108, which propagates along alpha1 and alpha5 toward the SAM~~-binding site. Although the overall secondary structures of the human and rat proteins are very similar (C(alpha) RMSD=0.4 A), several nonconserved residues are present in the SAM-(I89M, I91M, C95Y) and catechol- (C173V, R201M, E202K) binding sites. The human protein also contains three additional solvent-exposed cysteine residues (C95, C173, C188) that may contribute to intermolecular disulfide bond formation and protein aggregation.	+	The line below this paragraph, {{ABSTRACT_PUBMED_18486144}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 18486144 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_18486144}}

	==Disease==		==Disease==
Line 36:		Line 40:
	[[Category: Rossmann fold]]		[[Category: Rossmann fold]]
	[[Category: Sam]]		[[Category: Sam]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Wed Jun 4 09~~:54:32 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:44:39 2008''