3o7w - Revision history

OCA at 08:32, 20 March 2024

2024-03-20T08:32:58Z

← Older revision		Revision as of 08:32, 20 March 2024
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	==The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1==		==The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1==
	<StructureSection load='3o7w' size='340' side='right' caption='[[3o7w]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3o7w' size='340' side='right'caption='[[3o7w]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3o7w]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3O7W FirstGlance]. <br>		<table><tr><td colspan='2'>[[3o7w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3O7W FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 2Å</td></tr>
	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LCMT1, LCMT, CGI-68 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</td></tr>		<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></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=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [~~http~~://pdbe.org/3o7w PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3o7w PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7w 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=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [https://pdbe.org/3o7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [https://www.ebi.ac.uk/pdbsum/3o7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[~~[http~~://www.uniprot.org/uniprot/LCMT1_HUMAN LCMT1_HUMAN]] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.<ref>PMID:10600115</ref>		[https://www.uniprot.org/uniprot/LCMT1_HUMAN LCMT1_HUMAN] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.<ref>PMID:10600115</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=3o7w 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=3o7w ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	Leucine carboxyl methyltransferase 1 (LCMT1) methylates the terminal carboxyl group of the leucine 309 residue of human protein phosphatase 2A (PP2A). PP2A, a key regulator of many cellular processes, has recently generated additional interest as a potential cancer-therapeutic target. The status of PP2A methylation impacts upon the selection of the regulatory subunit by the PP2A core enzyme, thus directing its activity and subcellular localization. An X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet) has been solved to a resolution of 2 A. The structure enables the postulation of a mode of interaction with protein phosphatase PP2A and provides a platform for further functional studies of the regulation of methylation of PP2A.

	The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.,Tsai ML, Cronin N, Djordjevic S Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):14-24. Epub 2010, Dec 16. PMID:21206058<ref>PMID:21206058</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 3o7w" style="background-color:#fffaf0;"></div>~~
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Cronin, N~~]]		[[Category: Large Structures]]
	[[Category: ~~Djordjevic, S~~]]		[[Category: Cronin N]]
	[[Category: ~~Tsai, M L~~]]		[[Category: Djordjevic S]]
	[[Category: ~~Modified rossmann fold]]~~		[[Category: Tsai ML]]
	~~[[Category: Pp2a]]~~
	~~[[Category: Transferase~~]]

OCA at 09:41, 30 January 2019

2019-01-30T09:41:10Z

← Older revision		Revision as of 09:41, 30 January 2019
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/3o7w_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/3o7w_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>

OCA at 11:46, 5 August 2016

2016-08-05T11:46:16Z

← Older revision		Revision as of 11:46, 5 August 2016
Line 1:		Line 1:

	==The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1==		==The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1==
	<StructureSection load='3o7w' size='340' side='right' caption='[[3o7w]], [[Resolution\|resolution]] 2.00Å' scene=''>		<StructureSection load='3o7w' size='340' side='right' caption='[[3o7w]], [[Resolution\|resolution]] 2.00Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[3o7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O7W FirstGlance]. <br>		<table><tr><td colspan='2'>[[3o7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O7W FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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">LCMT1, LCMT, CGI-68 ([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">LCMT1, LCMT, CGI-68 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [http://www.ebi.ac.uk/pdbsum/3o7w 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=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [http://pdbe.org/3o7w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [http://www.ebi.ac.uk/pdbsum/3o7w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3o7w ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		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=3o7w ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 27:		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 3o7w" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Cronin, N]]		[[Category: Cronin, N]]
	[[Category: Djordjevic, S]]		[[Category: Djordjevic, S]]

OCA at 02:09, 25 December 2014

2014-12-25T02:09:34Z

← Older revision		Revision as of 02:09, 25 December 2014
Line 7:		Line 7:
	<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=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [http://www.ebi.ac.uk/pdbsum/3o7w 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=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [http://www.ebi.ac.uk/pdbsum/3o7w PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/LCMT1_HUMAN LCMT1_HUMAN]] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.<ref>PMID:10600115</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 06:25, 19 December 2014

2014-12-19T06:25:08Z

← Older revision		Revision as of 06:25, 19 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_3o7w\| PDB=3o7w \| SCENE= }}~~		==The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1==
	===The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1===		<StructureSection load='3o7w' size='340' side='right' caption='[[3o7w]], [[Resolution\|resolution]] 2.00Å' scene=''>
	~~{{ABSTRACT_PUBMED_21206058}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[3o7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O7W FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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">LCMT1, LCMT, CGI-68 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=3o7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o7w OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o7w RCSB], [http://www.ebi.ac.uk/pdbsum/3o7w 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/o7/3o7w_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 ==
			Leucine carboxyl methyltransferase 1 (LCMT1) methylates the terminal carboxyl group of the leucine 309 residue of human protein phosphatase 2A (PP2A). PP2A, a key regulator of many cellular processes, has recently generated additional interest as a potential cancer-therapeutic target. The status of PP2A methylation impacts upon the selection of the regulatory subunit by the PP2A core enzyme, thus directing its activity and subcellular localization. An X-ray crystal structure of human LCMT1 protein in complex with the cofactor S-adenosylmethionine (AdoMet) has been solved to a resolution of 2 A. The structure enables the postulation of a mode of interaction with protein phosphatase PP2A and provides a platform for further functional studies of the regulation of methylation of PP2A.

	~~==Function==~~		The structure of human leucine carboxyl methyltransferase 1 that regulates protein phosphatase PP2A.,Tsai ML, Cronin N, Djordjevic S Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):14-24. Epub 2010, Dec 16. PMID:21206058<ref>PMID:21206058</ref>
	~~[[http://www.uniprot.org/uniprot/LCMT1_HUMAN LCMT1_HUMAN]] Methylates the carboxyl group~~ of ~~the C-terminal~~ leucine ~~residue of~~ protein phosphatase ~~2A catalytic subunits to form alpha~~-~~leucine ester residues~~.<ref>PMID:~~10600115~~</ref>

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[3o7w]] is~~ a ~~1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes~~ the ~~now removed PDB entry [http://oca~~.~~weizmann~~.ac.il/~~oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA].~~		</div>
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:021206058</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Cronin, N.]]		[[Category: Cronin, N]]
	[[Category: Djordjevic, S.]]		[[Category: Djordjevic, S]]
	[[Category: Tsai, M L.]]		[[Category: Tsai, M L]]
	[[Category: Modified rossmann fold]]		[[Category: Modified rossmann fold]]
	[[Category: Pp2a]]		[[Category: Pp2a]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 07:42, 16 May 2013

2013-05-16T07:42:43Z

← Older revision		Revision as of 07:42, 16 May 2013
Line 1:		Line 1:
	~~[[Image:3o7w.png\|left\|200px]]~~

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_3o7w", 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_3o7w\| PDB=3o7w \| SCENE= }}		{{STRUCTURE_3o7w\| PDB=3o7w \| SCENE= }}

	===The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1===		===The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1===
			{{ABSTRACT_PUBMED_21206058}}

			==Function==
	~~<!--~~		[[http://www.uniprot.org/uniprot/LCMT1_HUMAN LCMT1_HUMAN]] Methylates the carboxyl group of the C-terminal leucine residue of protein phosphatase 2A catalytic subunits to form alpha-leucine ester residues.<ref>PMID:10600115</ref>
	~~The line below this paragraph, {{ABSTRACT_PUBMED_21206058}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov), where 21206058 is~~ the ~~PubMed ID number.~~
	-->
	~~{{ABSTRACT_PUBMED_21206058}}~~

	==About this Structure==		==About this Structure==
Line 22:		Line 10:

	==Reference==		==Reference==
	<ref group="xtra">PMID:021206058</ref><references group="xtra"/>		<ref group="xtra">PMID:021206058</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Cronin, N.]]		[[Category: Cronin, N.]]

OCA: Protected "3o7w" [edit=sysop:move=sysop]

2011-07-13T07:24:44Z

Protected "3o7w" [edit=sysop:move=sysop]

← Older revision	Revision as of 07:24, 13 July 2011
(No difference)

OCA at 07:24, 13 July 2011

2011-07-13T07:24:42Z

← Older revision		Revision as of 07:24, 13 July 2011
Line 1:		Line 1:
	~~{{Seed}}~~		[[Image:3o7w.png\|left\|200px]]
	[[Image:3o7w.~~jpg~~\|left\|200px]]

	<!--		<!--
Line 12:		Line 11:
	===The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1===		===The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1===


			<!--
			The line below this paragraph, {{ABSTRACT_PUBMED_21206058}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 21206058 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_21206058}}

	==About this Structure==		==About this Structure==
	~~3O7W~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA].		[[3o7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3mnt 3mnt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O7W OCA].

			==Reference==
			<ref group="xtra">PMID:021206058</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Cronin, N.]]		[[Category: Cronin, N.]]
Line 22:		Line 30:
	[[Category: Pp2a]]		[[Category: Pp2a]]
	[[Category: Transferase]]		[[Category: Transferase]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Sep 10 13:50:24 2010''~~

OCA at 09:41, 10 September 2010

2010-09-10T09:41:54Z

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{Seed}}
-The entry 3o7w is ON HOLD
+<!--
-Authors: Tsai, M.L., Cronin, N., Djordjevic, S.
+===The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1===
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 11 23:38:35 2010''
+==About this Structure==

OCA: New page: '''Unreleased structure''' The entry 3o7w is ON HOLD Authors: Tsai, M.L., Cronin, N., Djordjevic, S. Description: The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1 '...

2010-08-11T19:31:17Z

New page: '''Unreleased structure''' The entry 3o7w is ON HOLD Authors: Tsai, M.L., Cronin, N., Djordjevic, S. Description: The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1 '...

New page

'''Unreleased structure'''

The entry 3o7w is ON HOLD

Authors: Tsai, M.L., Cronin, N., Djordjevic, S.

Description: The Crystal Structure of Human Leucine Carboxyl Methyltransferase 1

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 11 23:38:35 2010''