2c0y - Revision history

OCA at 14:01, 13 December 2023

2023-12-13T14:01:09Z

←Older revision		Revision as of 14:01, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='2c0y' size='340' side='right'caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2c0y' size='340' side='right'caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat">~~<div style='overflow: auto; max~~-~~height: 3em;'>[[1bxf\|1bxf]]~~, [[~~1glo~~\|~~1glo~~]]~~, [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</div></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]] 2.1Å</td></tr>
-	~~<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en~~.~~wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [https://pdbe.org/2c0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [https://www.ebi.ac.uk/pdbsum/2c0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c0y 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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [https://pdbe.org/2c0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [https://www.ebi.ac.uk/pdbsum/2c0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c0y ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN]] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.	+	[https://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
	== 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: ~~Cathepsin S]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Hilgenfeld, R]]	+	[[Category: Hilgenfeld R]]
-	[[Category: Kaulmann, G]]	+	[[Category: Kaulmann G]]
-	[[Category: Palm~~, G J~~]]	+	[[Category: Palm GJ]]
-	[[Category: Schilling, K]]	+	[[Category: Schilling K]]
-	[[Category: Wiederanders, B]]	+	[[Category: Wiederanders B]]
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Lysosome]]~~	+
-	~~[[Category: Procathepsin s]]~~	+
-	~~[[Category: Proenzyme]]~~	+
-	~~[[Category: Prosegment binding loop]]~~	+
-	~~[[Category: Protease]]~~	+
-	~~[[Category: Proteinase]]~~	+
-	~~[[Category: Thiol protease]]~~	+
-	~~[[Category: Zymogen~~]]	+

OCA at 09:45, 5 May 2021

2021-05-05T09:45:39Z

←Older revision		Revision as of 09:45, 5 May 2021
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	<StructureSection load='2c0y' size='340' side='right'caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2c0y' size='340' side='right'caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bxf\|1bxf]], [[1glo\|1glo]], [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bxf\|1bxf]], [[1glo\|1glo]], [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [~~http~~://pdbe.org/2c0y PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2c0y PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2c0y 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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [https://pdbe.org/2c0y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [https://www.ebi.ac.uk/pdbsum/2c0y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c0y ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN]] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.	+	[[https://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN]] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 06:23, 29 May 2019

2019-05-29T06:23:59Z

←Older revision		Revision as of 06:23, 29 May 2019
Line 31:		Line 31:

	==See Also==		==See Also==
-	*[[Cathepsin\|Cathepsin]]	+	*[[Cathepsin 3D structures\|Cathepsin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:22, 3 April 2019

2019-04-03T07:22:42Z

←Older revision		Revision as of 07:22, 3 April 2019
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	==THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S==		==THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S==
-	<StructureSection load='2c0y' size='340' side='right' caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='2c0y' size='340' side='right'caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>		<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>
Line 38:		Line 38:
	[[Category: Cathepsin S]]		[[Category: Cathepsin S]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Hilgenfeld, R]]		[[Category: Hilgenfeld, R]]
	[[Category: Kaulmann, G]]		[[Category: Kaulmann, G]]

OCA at 08:00, 23 May 2018

2018-05-23T08:00:25Z

←Older revision		Revision as of 08:00, 23 May 2018
Line 1:		Line 1:
		+
	==THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S==		==THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S==
	<StructureSection load='2c0y' size='340' side='right' caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2c0y' size='340' side='right' caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>
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	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bxf\|1bxf]], [[1glo\|1glo]], [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bxf\|1bxf]], [[1glo\|1glo]], [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [http://pdbe.org/2c0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [http://www.ebi.ac.uk/pdbsum/2c0y 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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [http://pdbe.org/2c0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [http://www.ebi.ac.uk/pdbsum/2c0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2c0y ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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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/c0/2c0y_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c0/2c0y_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>
	</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=2c0y ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 13:31, 11 September 2015

2015-09-11T13:31:12Z

←Older revision		Revision as of 13:31, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='2c0y' size='340' side='right' caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='2c0y' size='340' side='right' caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bxf\|1bxf]], [[1glo\|1glo]], [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bxf\|1bxf]], [[1glo\|1glo]], [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [http://www.ebi.ac.uk/pdbsum/2c0y 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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [http://pdbe.org/2c0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [http://www.ebi.ac.uk/pdbsum/2c0y PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	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 2c0y" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Cathepsin S]]		[[Category: Cathepsin S]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Hilgenfeld, R]]		[[Category: Hilgenfeld, R]]
	[[Category: Kaulmann, G]]		[[Category: Kaulmann, G]]

OCA at 17:06, 25 December 2014

2014-12-25T17:06:32Z

←Older revision		Revision as of 17:06, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>		<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bxf\|1bxf]], [[1glo\|1glo]], [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bxf\|1bxf]], [[1glo\|1glo]], [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [http://www.ebi.ac.uk/pdbsum/2c0y 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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [http://www.ebi.ac.uk/pdbsum/2c0y PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CATS_HUMAN CATS_HUMAN]] Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	[[Category: Cathepsin S]]		[[Category: Cathepsin S]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Hilgenfeld, R.]]	+	[[Category: Hilgenfeld, R]]
-	[[Category: Kaulmann, G.]]	+	[[Category: Kaulmann, G]]
-	[[Category: Palm, G J.]]	+	[[Category: Palm, G J]]
-	[[Category: Schilling, K.]]	+	[[Category: Schilling, K]]
-	[[Category: Wiederanders, B.]]	+	[[Category: Wiederanders, B]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 04:26, 29 September 2014

2014-09-29T04:26:35Z

←Older revision		Revision as of 04:26, 29 September 2014
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-	[[~~Image:~~2c0y.~~png~~\|~~left~~\|200px]]	+	==THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S==
		+	<StructureSection load='2c0y' size='340' side='right' caption='[[2c0y]], [[Resolution\|resolution]] 2.10Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2c0y]] 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=2C0Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2C0Y FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bxf\|1bxf]], [[1glo\|1glo]], [[1ms6\|1ms6]], [[1npz\|1npz]], [[1nqc\|1nqc]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cathepsin_S Cathepsin S], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.27 3.4.22.27] </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=2c0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c0y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2c0y RCSB], [http://www.ebi.ac.uk/pdbsum/2c0y 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/c0/2c0y_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 ==
		+	The crystal structure of the active-site mutant Cys25 --> Ala of glycosylated human procathepsin S is reported. It was determined by molecular replacement and refined to 2.1 Angstrom resolution, with an R-factor of 0.198. The overall structure is very similar to other cathepsin L-like zymogens of the C1A clan. The peptidase unit comprises two globular domains, and a small third domain is formed by the N-terminal part of the prosequence. It is anchored to the prosegment binding loop of the enzyme. Prosegment residues beyond the prodomain dock to the substrate binding cleft in a nonproductive orientation. Structural comparison with published data for mature cathepsin S revealed that procathepsin S residues Phe146, Phe70, and Phe211 adopt different orientations. Being part of the S1' and S2 pockets, they may contribute to the selectivity of ligand binding. Regarding the prosequence, length, orientation and anchoring of helix alpha3p differ from related zymogens, thereby possibly contributing to the specificity of propeptide-enzyme interaction in the papain family. The discussion focuses on the functional importance of the most conserved residues in the prosequence for structural integrity, inhibition and folding assistance, considering scanning mutagenesis data published for procathepsin S and for its isolated propeptide.

-	~~{{STRUCTURE_2c0y\| PDB=2c0y \| SCENE= }}~~	+	The crystal structure of a Cys25 -> Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions.,Kaulmann G, Palm GJ, Schilling K, Hilgenfeld R, Wiederanders B Protein Sci. 2006 Nov;15(11):2619-29. PMID:17075137<ref>PMID:17075137</ref>

-	~~===THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_17075137}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[2c0y]] 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=2C0Y OCA].~~	+

	==See Also==		==See Also==
	*[[Cathepsin\|Cathepsin]]		*[[Cathepsin\|Cathepsin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:017075137<~~/~~ref~~><~~ref group="xtra">PMID:009655332</ref><ref group="xtra">PMID:011856830</ref><ref group="xtra">PMID:012641451</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Cathepsin S]]		[[Category: Cathepsin S]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 19:15, 20 October 2012

2012-10-20T19:15:32Z

←Older revision		Revision as of 19:15, 20 October 2012
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	==About this Structure==		==About this Structure==
-	[[2c0y]] is a 1 chain structure ~~of [[Cathepsin]]~~ 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=2C0Y OCA].	+	[[2c0y]] 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=2C0Y OCA].

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

OCA at 06:45, 27 July 2012

2012-07-27T06:45:57Z

←Older revision		Revision as of 06:45, 27 July 2012
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	[[Image:2c0y.png\|left\|200px]]		[[Image:2c0y.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_2c0y\| PDB=2c0y \| SCENE= }}		{{STRUCTURE_2c0y\| PDB=2c0y \| SCENE= }}

	===THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S===		===THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S===

-
-	<!--
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	==See Also==		==See Also==
-	*[[Cathepsin]]	+	*[[Cathepsin\|Cathepsin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~17075137~~</ref><ref group="xtra">PMID:~~9655332~~</ref><ref group="xtra">PMID:~~11856830~~</ref><ref group="xtra">PMID:~~12641451~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:017075137</ref><ref group="xtra">PMID:009655332</ref><ref group="xtra">PMID:011856830</ref><ref group="xtra">PMID:012641451</ref><references group="xtra"/>
	[[Category: Cathepsin S]]		[[Category: Cathepsin S]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]