4p7j - Revision history

OCA at 00:40, 28 December 2023

OCA — Thu, 28 Dec 2023 00:40:59 GMT

←Older revision		Revision as of 00:40, 28 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4p7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P7J FirstGlance]. <br>		<table><tr><td colspan='2'>[[4p7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P7J FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.45Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [https://pdbe.org/4p7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [https://www.ebi.ac.uk/pdbsum/4p7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p7j 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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [https://pdbe.org/4p7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [https://www.ebi.ac.uk/pdbsum/4p7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p7j ProSAT]</span></td></tr>
	</table>		</table>

OCA at 12:45, 1 February 2023

OCA — Wed, 01 Feb 2023 12:45:43 GMT

←Older revision		Revision as of 12:45, 1 February 2023
Line 3:		Line 3:
	<StructureSection load='4p7j' size='340' side='right'caption='[[4p7j]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='4p7j' size='340' side='right'caption='[[4p7j]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4p7j]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Buffalo_rat Buffalo rat~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P7J OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4P7J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4p7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P7J FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p7k\|4p7k]], [[4p7f\|4p7f]], [[4p7g\|4p7g]]</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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [https://pdbe.org/4p7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [https://www.ebi.ac.uk/pdbsum/4p7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p7j ProSAT]</span></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=10116 Buffalo rat])</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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [~~http~~://pdbe.org/4p7j PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4p7j PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4p7j ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/COMT_RAT COMT_RAT]] 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_RAT COMT_RAT] 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 20:

	==See Also==		==See Also==
-	*[[Catechol O-methyltransferase\|Catechol O-methyltransferase]]	+	*[[Catechol O-methyltransferase 3D structures\|Catechol O-methyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Buffalo rat]]
-	[[Category: Catechol O-methyltransferase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Benz, J]]	+	[[Category: Rattus norvegicus]]
-	[[Category: Ehler, A]]	+	[[Category: Benz J]]
-	[[Category: Rudolph~~, M G~~]]	+	[[Category: Ehler A]]
-	[[Category: Schlatter, D]]	+	[[Category: Rudolph MG]]
-	~~[[Category: Alternative initiation]]~~	+	[[Category: Schlatter D]]
-	~~[[Category: Catecholamine metabolism]]~~	+
-	~~[[Category: Cell membrane]]~~	+
-	~~[[Category: Conformational change]]~~	+
-	~~[[Category: Enzyme mechanism]]~~	+
-	~~[[Category: Metal-binding]]~~	+
-	~~[[Category: Methyltransferase]]~~	+
-	~~[[Category: Neurotransmitter degradation]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: S-adenosyl-l-methionine]]~~	+
-	~~[[Category: Signal-anchor]]~~	+
-	~~[[Category: Transferase]]~~	+
-	~~[[Category: Transmembrane anchor~~]]	+

OCA at 08:04, 17 April 2019

OCA — Wed, 17 Apr 2019 08:04:32 GMT

←Older revision		Revision as of 08:04, 17 April 2019
Line 1:		Line 1:

	==Rat apo-COMT sulfate bound==		==Rat apo-COMT sulfate bound==
-	<StructureSection load='4p7j' size='340' side='right' caption='[[4p7j]], [[Resolution\|resolution]] 1.45Å' scene=''>	+	<StructureSection load='4p7j' size='340' side='right'caption='[[4p7j]], [[Resolution\|resolution]] 1.45Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4p7j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P7J FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4p7j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P7J FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p7k\|4p7k]], [[4p7f\|4p7f]], [[4p7g\|4p7g]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p7k\|4p7k]], [[4p7f\|4p7f]], [[4p7g\|4p7g]]</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=10116 Buffalo rat])</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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [http://pdbe.org/4p7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [http://www.ebi.ac.uk/pdbsum/4p7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p7j 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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [http://pdbe.org/4p7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [http://www.ebi.ac.uk/pdbsum/4p7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p7j ProSAT]</span></td></tr>
Line 27:		Line 28:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Buffalo rat]]
	[[Category: Catechol O-methyltransferase]]		[[Category: Catechol O-methyltransferase]]
		+	[[Category: Large Structures]]
	[[Category: Benz, J]]		[[Category: Benz, J]]
	[[Category: Ehler, A]]		[[Category: Ehler, A]]

OCA at 12:08, 11 August 2016

OCA — Thu, 11 Aug 2016 12:08:22 GMT

←Older revision		Revision as of 12:08, 11 August 2016
Line 1:		Line 1:
		+
	==Rat apo-COMT sulfate bound==		==Rat apo-COMT sulfate bound==
	<StructureSection load='4p7j' size='340' side='right' caption='[[4p7j]], [[Resolution\|resolution]] 1.45Å' scene=''>		<StructureSection load='4p7j' size='340' side='right' caption='[[4p7j]], [[Resolution\|resolution]] 1.45Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p7k\|4p7k]], [[4p7f\|4p7f]], [[4p7g\|4p7g]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p7k\|4p7k]], [[4p7f\|4p7f]], [[4p7g\|4p7g]]</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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [http://www.ebi.ac.uk/pdbsum/4p7j 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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [http://pdbe.org/4p7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [http://www.ebi.ac.uk/pdbsum/4p7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p7j ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	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 4p7j" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Catechol O-methyltransferase\|Catechol O-methyltransferase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:30, 24 December 2014

OCA — Wed, 24 Dec 2014 15:30:47 GMT

←Older revision		Revision as of 15:30, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4p7j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P7J FirstGlance]. <br>		<table><tr><td colspan='2'>[[4p7j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P7J FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p7k\|4p7k]], [[4p7f\|4p7f]], [[4p7g\|4p7g]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p7k\|4p7k]], [[4p7f\|4p7f]], [[4p7g\|4p7g]]</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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [http://www.ebi.ac.uk/pdbsum/4p7j 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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [http://www.ebi.ac.uk/pdbsum/4p7j PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/COMT_RAT COMT_RAT]] 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.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Catechol O-methyltransferase]]		[[Category: Catechol O-methyltransferase]]
-	[[Category: Benz, J.]]	+	[[Category: Benz, J]]
-	[[Category: Ehler, A.]]	+	[[Category: Ehler, A]]
-	[[Category: Rudolph, M G.]]	+	[[Category: Rudolph, M G]]
-	[[Category: Schlatter, D.]]	+	[[Category: Schlatter, D]]
	[[Category: Alternative initiation]]		[[Category: Alternative initiation]]
	[[Category: Catecholamine metabolism]]		[[Category: Catecholamine metabolism]]

OCA at 06:14, 13 August 2014

OCA — Wed, 13 Aug 2014 06:14:46 GMT

←Older revision		Revision as of 06:14, 13 August 2014
Line 8:		Line 8:
	<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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [http://www.ebi.ac.uk/pdbsum/4p7j PDBsum]</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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [http://www.ebi.ac.uk/pdbsum/4p7j PDBsum]</span></td></tr>
	<table>		<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Methylation catalysed by catechol-O-methyltransferase (COMT) is the main pathway of catechol neurotransmitter deactivation in the prefrontal cortex. Low levels of this class of neurotransmitters are held to be causative of diseases such as schizophrenia, depression and Parkinson's disease. Inhibition of COMT may increase neurotransmitter levels, thus offering a route for treatment. Structure-based drug design hitherto seems to be based on the closed enzyme conformation. Here, a set of apo, semi-holo, holo and Michaelis form crystal structures are described that define the conformational space available to COMT and that include likely intermediates along the catalytic pathway. Domain swaps and sizeable loop movements around the active site testify to the flexibility of this enzyme, rendering COMT a difficult drug target. The low affinity of the co-substrate S-adenosylmethionine and the large conformational changes involved during catalysis highlight significant energetic investment to achieve the closed conformation. Since each conformation of COMT is a bona fide target for inhibitors, other states than the closed conformation may be promising to address. Crystallographic data for an alternative avenue of COMT inhibition, i.e. locking of the apo state by an inhibitor, are presented. The set of COMT structures may prove to be useful for the development of novel classes of inhibitors.
		+
		+	Mapping the conformational space accessible to catechol-O-methyltransferase.,Ehler A, Benz J, Schlatter D, Rudolph MG Acta Crystallogr D Biol Crystallogr. 2014 Aug 1;70(Pt 8):2163-74. doi:, 10.1107/S1399004714012917. Epub 2014 Jul 25. PMID:25084335<ref>PMID:25084335</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:18, 18 June 2014

OCA — Wed, 18 Jun 2014 08:18:18 GMT

←Older revision		Revision as of 08:18, 18 June 2014
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-	'''~~Unreleased structure~~'''	+	==Rat apo-COMT sulfate bound==
-		+	<StructureSection load='4p7j' size='340' side='right' caption='[[4p7j]], [[Resolution\|resolution]] 1.45Å' scene=''>
-	~~The entry~~ 4p7j is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4p7j]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P7J FirstGlance]. <br>
-	~~Authors~~: ~~Ehler~~, A., ~~Benz~~, J., ~~Schlatter~~, D., Rudolph, M.G.	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene><br>
-		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4p7k\|4p7k]], [[4p7f\|4p7f]], [[4p7g\|4p7g]]</td></tr>
-	~~Description~~: ~~Rat apo~~-~~COMT sulfate bound~~	+	<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=4p7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p7j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4p7j RCSB], [http://www.ebi.ac.uk/pdbsum/4p7j PDBsum]</span></td></tr>
		+	<table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Catechol O-methyltransferase]]
		+	[[Category: Benz, J.]]
		+	[[Category: Ehler, A.]]
		+	[[Category: Rudolph, M G.]]
		+	[[Category: Schlatter, D.]]
		+	[[Category: Alternative initiation]]
		+	[[Category: Catecholamine metabolism]]
		+	[[Category: Cell membrane]]
		+	[[Category: Conformational change]]
		+	[[Category: Enzyme mechanism]]
		+	[[Category: Metal-binding]]
		+	[[Category: Methyltransferase]]
		+	[[Category: Neurotransmitter degradation]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: S-adenosyl-l-methionine]]
		+	[[Category: Signal-anchor]]
		+	[[Category: Transferase]]
		+	[[Category: Transmembrane anchor]]

OCA at 07:48, 11 June 2014

OCA — Wed, 11 Jun 2014 07:48:54 GMT

←Older revision		Revision as of 07:48, 11 June 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4p7j is ON HOLD ~~until Paper Publication~~	+	The entry 4p7j is ON HOLD

	Authors: Ehler, A., Benz, J., Schlatter, D., Rudolph, M.G.		Authors: Ehler, A., Benz, J., Schlatter, D., Rudolph, M.G.

	Description: Rat apo-COMT sulfate bound		Description: Rat apo-COMT sulfate bound

OCA at 07:22, 23 April 2014

OCA — Wed, 23 Apr 2014 07:22:47 GMT

←Older revision		Revision as of 07:22, 23 April 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4p7j is ON HOLD	+	The entry 4p7j is ON HOLD until Paper Publication

	Authors: Ehler, A., Benz, J., Schlatter, D., Rudolph, M.G.		Authors: Ehler, A., Benz, J., Schlatter, D., Rudolph, M.G.

	Description: Rat apo-COMT sulfate bound		Description: Rat apo-COMT sulfate bound

OCA at 05:53, 9 April 2014

OCA — Wed, 09 Apr 2014 05:53:06 GMT

←Older revision		Revision as of 05:53, 9 April 2014
Line 3:		Line 3:
	The entry 4p7j is ON HOLD		The entry 4p7j is ON HOLD

-	Authors: ~~see citation~~	+	Authors: Ehler, A., Benz, J., Schlatter, D., Rudolph, M.G.

-	Description: ~~rat~~ apo-COMT sulfate bound	+	Description: Rat apo-COMT sulfate bound