1o6f - Revision history

OCA at 12:29, 13 December 2023

2023-12-13T12:29:01Z

←Older revision		Revision as of 12:29, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='1o6f' size='340' side='right'caption='[[1o6f]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='1o6f' size='340' side='right'caption='[[1o6f]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1o6f]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Pig Pig~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=1O6F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1o6f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O6F FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GLY:GLYCINE'>GLY</scene>~~, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</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]] 1.6Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td><~~td class~~=~~"sblockDat">PREP ([http~~:~~//www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [https://pdbe.org/1o6f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [https://www.ebi.ac.uk/pdbsum/1o6f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6f ProSAT]</span></td></tr>
-	<~~tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26]~~ </~~span~~></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [~~http~~://pdbe.org/1o6f PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1o6f PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6f ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/PPCE_PIG PPCE_PIG]] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.	+	[https://www.uniprot.org/uniprot/PPCE_PIG PPCE_PIG] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Pig]]~~	+	[[Category: Sus scrofa]]
-	~~[[Category: Prolyl oligopeptidase~~]]	+	[[Category: Fulop V]]
-	[[Category: Fulop, V]]	+	[[Category: Rea D]]
-	[[Category: Rea, D]]	+
-	~~[[Category: Alpha/ beta-hydrolase]]~~	+
-	~~[[Category: Amnesia]]~~	+
-	~~[[Category: Beta-propeller]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 09:04, 2 December 2020

2020-12-02T09:04:52Z

←Older revision		Revision as of 09:04, 2 December 2020
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	==PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO==		==PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO==
-	<StructureSection load='1o6f' size='340' side='right' caption='[[1o6f]], [[Resolution\|resolution]] 1.60Å' scene=''>	+	<StructureSection load='1o6f' size='340' side='right'caption='[[1o6f]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1o6f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1O6F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1o6f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1O6F FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</div></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PREP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PREP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://pdbe.org/1o6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6f ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://pdbe.org/1o6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Pig]]		[[Category: Pig]]
	[[Category: Prolyl oligopeptidase]]		[[Category: Prolyl oligopeptidase]]

OCA at 07:01, 12 December 2018

2018-12-12T07:01:03Z

←Older revision		Revision as of 07:01, 12 December 2018
Line 3:		Line 3:
	<StructureSection load='1o6f' size='340' side='right' caption='[[1o6f]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='1o6f' size='340' side='right' caption='[[1o6f]], [[Resolution\|resolution]] 1.60Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1o6f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O6F FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1o6f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O6F FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PREP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9823 PIG])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://pdbe.org/1o6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6f 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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://pdbe.org/1o6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6f ProSAT]</span></td></tr>
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Pig]]
	[[Category: Prolyl oligopeptidase]]		[[Category: Prolyl oligopeptidase]]
	[[Category: Fulop, V]]		[[Category: Fulop, V]]

OCA at 05:58, 20 June 2018

2018-06-20T05:58:56Z

←Older revision		Revision as of 05:58, 20 June 2018
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	</div>		</div>
	<div class="pdbe-citations 1o6f" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1o6f" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Prolyl Endopeptidase\|Prolyl Endopeptidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:01, 7 February 2018

2018-02-07T07:01:25Z

←Older revision		Revision as of 07:01, 7 February 2018
Line 1:		Line 1:
		+
	==PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO==		==PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO==
	<StructureSection load='1o6f' size='340' side='right' caption='[[1o6f]], [[Resolution\|resolution]] 1.60Å' scene=''>		<StructureSection load='1o6f' size='340' side='right' caption='[[1o6f]], [[Resolution\|resolution]] 1.60Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://pdbe.org/1o6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f 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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://pdbe.org/1o6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1o6f ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 14:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o6/1o6f_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o6/1o6f_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 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1o6f" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1o6f" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Prolyl Endopeptidase\|Prolyl Endopeptidase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 02:31, 10 February 2016

2016-02-10T02:31:04Z

←Older revision		Revision as of 02:31, 10 February 2016
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=1o6f ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:30, 11 September 2015

2015-09-11T04:30:10Z

←Older revision		Revision as of 04:30, 11 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f 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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://pdbe.org/1o6f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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 1o6f" style="background-color:#fffaf0;"></div>

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

OCA at 11:09, 25 December 2014

2014-12-25T11:09:48Z

←Older revision		Revision as of 11:09, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1o6f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O6F FirstGlance]. <br>		<table><tr><td colspan='2'>[[1o6f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O6F FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f 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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PPCE_PIG PPCE_PIG]] Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Prolyl oligopeptidase]]		[[Category: Prolyl oligopeptidase]]
-	[[Category: Fulop, V.]]	+	[[Category: Fulop, V]]
-	[[Category: Rea, D.]]	+	[[Category: Rea, D]]
	[[Category: Alpha/ beta-hydrolase]]		[[Category: Alpha/ beta-hydrolase]]
	[[Category: Amnesia]]		[[Category: Amnesia]]
	[[Category: Beta-propeller]]		[[Category: Beta-propeller]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
-	[[Category: Prolyl oligopeptidase]]

OCA at 13:51, 29 September 2014

2014-09-29T13:51:28Z

←Older revision		Revision as of 13:51, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1o6f\| PDB=1o6f \| SCENE= }}~~	+	==PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO==
-	===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO===	+	<StructureSection load='1o6f' size='340' side='right' caption='[[1o6f]], [[Resolution\|resolution]] 1.60Å' scene=''>
-	~~{{ABSTRACT_PUBMED_12228249}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1o6f]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O6F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1O6F FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1e5t\|1e5t]], [[1e8m\|1e8m]], [[1e8n\|1e8n]], [[1h2w\|1h2w]], [[1h2x\|1h2x]], [[1h2y\|1h2y]], [[1h2z\|1h2z]], [[1o6g\|1o6g]], [[1qfm\|1qfm]], [[1qfs\|1qfs]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_oligopeptidase Prolyl oligopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.26 3.4.21.26] </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=1o6f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o6f OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1o6f RCSB], [http://www.ebi.ac.uk/pdbsum/1o6f 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/o6/1o6f_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 ==
		+	Prolyl oligopeptidase, a serine peptidase unrelated to trypsin and subtilisin, is implicated in memory disorders and is an important target of drug design. The catalytic competence of the Asp(641) residue of the catalytic triad (Ser(554), Asp(641), His(680)) was studied using the D641N and D641A variants of the enzyme. Both variants displayed 3 orders of magnitude reduction in k(cat)/K(m) for benzyloxycarbonyl-Gly-Pro-2-naphthylamide. Using an octapeptide substrate, the decrease was 6 orders of magnitude, whereas with Z-Gly-Pro-4-nitrophenyl ester there was virtually no change in k(cat)/K(m). This indicates that the contribution of Asp(641) is very much dependent on the substrate-leaving group, which was not the case for the classic serine peptidase, trypsin. The rate constant for benzyloxycarbonyl-Gly-Pro-thiobenzylester conformed to this series as demonstrated by a method designed for monitoring the hydrolysis of thiolesters in the presence of thiol groups. Alkylation of His(680) with Z-Gly-Pro-CH(2)Cl was concluded with similar rate constants for wild-type and D641A variant. However, kinetic measurements with Z-Gly-Pro-OH, a product-like inhibitor, indicated that the His(680) is not accessible in the enzyme variants. Crystal structure determination of these mutants revealed subtle perturbations related to the catalytic activity. Many of these observations show differences in the catalysis between trypsin and prolyl oligopeptidase.

-	~~==About this Structure==~~	+	Substrate-dependent competency of the catalytic triad of prolyl oligopeptidase.,Szeltner Z, Rea D, Juhasz T, Renner V, Mucsi Z, Orosz G, Fulop V, Polgar L J Biol Chem. 2002 Nov 22;277(47):44597-605. Epub 2002 Sep 11. PMID:12228249<ref>PMID:12228249</ref>
-	~~[[1o6f]] is a 1 chain structure~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=1O6F OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Prolyl Endopeptidase\|Prolyl Endopeptidase]]		*[[Prolyl Endopeptidase\|Prolyl Endopeptidase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:012228249<~~/~~ref~~><~~ref group="xtra">PMID:011031266</ref><ref group="xtra">PMID:011256612</ref><ref group="xtra">PMID:009695945</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Prolyl oligopeptidase]]		[[Category: Prolyl oligopeptidase]]
	[[Category: Fulop, V.]]		[[Category: Fulop, V.]]

OCA at 09:09, 11 March 2013

2013-03-11T09:09:12Z

←Older revision		Revision as of 09:09, 11 March 2013
Line 1:		Line 1:
-	[[Image:1o6f.png\|left\|200px]]
-
	{{STRUCTURE_1o6f\| PDB=1o6f \| SCENE= }}		{{STRUCTURE_1o6f\| PDB=1o6f \| SCENE= }}
-
	===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO===		===PROLYL OLIGOPEPTIDASE FROM PORCINE BRAIN, D641A MUTANT WITH BOUND PEPTIDE LIGAND SUC-GLY-PRO===
-
	{{ABSTRACT_PUBMED_12228249}}		{{ABSTRACT_PUBMED_12228249}}