3k0o - Revision history

OCA at 08:07, 6 September 2023

OCA — Wed, 06 Sep 2023 08:07:19 GMT

←Older revision		Revision as of 08:07, 6 September 2023
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	<StructureSection load='3k0o' size='340' side='right'caption='[[3k0o]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='3k0o' size='340' side='right'caption='[[3k0o]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3k0o]] 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=3K0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K0O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3k0o]] 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=3K0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K0O 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;'>[[3k0m\|3k0m]], [[3k0n\|3k0n]], [[3k0p\|3k0p]], [[3k0q\|3k0q]], [[3k0r\|3k0r]]</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]] 1.55Å</td></tr>
-	~~<tr~~ id~~='gene'><td class~~="~~sblockLbl~~">~~<b>~~[[~~Gene~~\|~~Gene:~~]]~~</b></td><td class="sblockDat">PPIA, CYPA ([https://www~~.~~ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info~~&~~srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [https://pdbe.org/3k0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [https://www.ebi.ac.uk/pdbsum/3k0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k0o 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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [https://pdbe.org/3k0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [https://www.ebi.ac.uk/pdbsum/3k0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k0o ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.	+	[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
	== 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: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Peptidylprolyl isomerase]]~~	+	[[Category: Alber T]]
-	[[Category: Alber, T]]	+	[[Category: Fraser JS]]
-	[[Category: Fraser~~, J S]]~~	+
-	~~[[Category: Cyclosporin]]~~	+
-	~~[[Category: Host-virus interaction]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Isopeptide bond]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Proline isomerase]]~~	+
-	~~[[Category: Rotamase~~]]	+

OCA at 12:19, 13 October 2021

OCA — Wed, 13 Oct 2021 12:19:48 GMT

←Older revision		Revision as of 12:19, 13 October 2021
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	==Room temperature structure of CypA mutant Ser99Thr==		==Room temperature structure of CypA mutant Ser99Thr==
-	<StructureSection load='3k0o' size='340' side='right' caption='[[3k0o]], [[Resolution\|resolution]] 1.55Å' scene=''>	+	<StructureSection load='3k0o' size='340' side='right'caption='[[3k0o]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3k0o]] 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=3K0O OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3K0O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3k0o]] 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=3K0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K0O FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k0m\|3k0m]], [[3k0n\|3k0n]], [[3k0p\|3k0p]], [[3k0q\|3k0q]], [[3k0r\|3k0r]]</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;'>[[3k0m\|3k0m]], [[3k0n\|3k0n]], [[3k0p\|3k0p]], [[3k0q\|3k0q]], [[3k0r\|3k0r]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [~~http~~://pdbe.org/3k0o PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3k0o PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3k0o 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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [https://pdbe.org/3k0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [https://www.ebi.ac.uk/pdbsum/3k0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k0o ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.	+	[[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:

	==See Also==		==See Also==
-	*[[Cyclophilin\|Cyclophilin]]	+	*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 38:		Line 38:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Alber, T]]		[[Category: Alber, T]]

OCA at 09:34, 26 December 2018

OCA — Wed, 26 Dec 2018 09:34:57 GMT

←Older revision		Revision as of 09:34, 26 December 2018
Line 1:		Line 1:
		+
	==Room temperature structure of CypA mutant Ser99Thr==		==Room temperature structure of CypA mutant Ser99Thr==
	<StructureSection load='3k0o' size='340' side='right' caption='[[3k0o]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='3k0o' size='340' side='right' caption='[[3k0o]], [[Resolution\|resolution]] 1.55Å' scene=''>
Line 6:		Line 7:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [http://pdbe.org/3k0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [http://www.ebi.ac.uk/pdbsum/3k0o 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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [http://pdbe.org/3k0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [http://www.ebi.ac.uk/pdbsum/3k0o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k0o 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/k0/3k0o_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/k0/3k0o_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 13:40, 7 February 2016

OCA — Sun, 07 Feb 2016 13:40:14 GMT

←Older revision		Revision as of 13:40, 7 February 2016
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	<StructureSection load='3k0o' size='340' side='right' caption='[[3k0o]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='3k0o' size='340' side='right' caption='[[3k0o]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3k0o]] 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=3K0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K0O FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3k0o]] 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=3K0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K0O FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k0m\|3k0m]], [[3k0n\|3k0n]], [[3k0p\|3k0p]], [[3k0q\|3k0q]], [[3k0r\|3k0r]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k0m\|3k0m]], [[3k0n\|3k0n]], [[3k0p\|3k0p]], [[3k0q\|3k0q]], [[3k0r\|3k0r]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([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">PPIA, CYPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [http://www.ebi.ac.uk/pdbsum/3k0o 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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [http://pdbe.org/3k0o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [http://www.ebi.ac.uk/pdbsum/3k0o PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 18:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3k0o ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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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 3k0o" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Alber, T]]		[[Category: Alber, T]]

OCA at 15:29, 24 December 2014

OCA — Wed, 24 Dec 2014 15:29:19 GMT

←Older revision		Revision as of 15:29, 24 December 2014
Line 8:		Line 8:
	<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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [http://www.ebi.ac.uk/pdbsum/3k0o 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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [http://www.ebi.ac.uk/pdbsum/3k0o PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 16:20, 18 December 2014

OCA — Thu, 18 Dec 2014 16:20:57 GMT

←Older revision		Revision as of 16:20, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3k0o~~\| ~~PDB~~=3k0o \| ~~SCENE~~= }}	+	==Room temperature structure of CypA mutant Ser99Thr==
-	===~~Room temperature~~ structure of ~~CypA mutant Ser99Thr~~===	+	<StructureSection load='3k0o' size='340' side='right' caption='[[3k0o]], [[Resolution\|resolution]] 1.55Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19956261}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3k0o]] 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=3K0O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K0O FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3k0m\|3k0m]], [[3k0n\|3k0n]], [[3k0p\|3k0p]], [[3k0q\|3k0q]], [[3k0r\|3k0r]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">PPIA, CYPA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </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=3k0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k0o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3k0o RCSB], [http://www.ebi.ac.uk/pdbsum/3k0o 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/k0/3k0o_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 ==
		+	A long-standing challenge is to understand at the atomic level how protein dynamics contribute to enzyme catalysis. X-ray crystallography can provide snapshots of conformational substates sampled during enzymatic reactions, while NMR relaxation methods reveal the rates of interconversion between substates and the corresponding relative populations. However, these current methods cannot simultaneously reveal the detailed atomic structures of the rare states and rationalize the finding that intrinsic motions in the free enzyme occur on a timescale similar to the catalytic turnover rate. Here we introduce dual strategies of ambient-temperature X-ray crystallographic data collection and automated electron-density sampling to structurally unravel interconverting substates of the human proline isomerase, cyclophilin A (CYPA, also known as PPIA). A conservative mutation outside the active site was designed to stabilize features of the previously hidden minor conformation. This mutation not only inverts the equilibrium between the substates, but also causes large, parallel reductions in the conformational interconversion rates and the catalytic rate. These studies introduce crystallographic approaches to define functional minor protein conformations and, in combination with NMR analysis of the enzyme dynamics in solution, show how collective motions directly contribute to the catalytic power of an enzyme.

-	~~==Function==~~	+	Hidden alternative structures of proline isomerase essential for catalysis.,Fraser JS, Clarkson MW, Degnan SC, Erion R, Kern D, Alber T Nature. 2009 Dec 3;462(7273):669-73. PMID:19956261<ref>PMID:19956261</ref>
-	~~[[http://www~~.~~uniprot~~.~~org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis~~-~~trans isomerization of proline imidic peptide bonds in oligopeptides~~.	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3k0o]] 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=3K0O OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:019956261</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Cyclophilin\|Cyclophilin]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
-	[[Category: Alber, T.]]	+	[[Category: Alber, T]]
-	[[Category: Fraser, J S.]]	+	[[Category: Fraser, J S]]
	[[Category: Cyclosporin]]		[[Category: Cyclosporin]]
	[[Category: Host-virus interaction]]		[[Category: Host-virus interaction]]

OCA at 09:01, 19 June 2013

OCA — Wed, 19 Jun 2013 09:01:43 GMT

←Older revision		Revision as of 09:01, 19 June 2013
Line 1:		Line 1:
-	[[Image:3k0o.png\|left\|200px]]
-
	{{STRUCTURE_3k0o\| PDB=3k0o \| SCENE= }}		{{STRUCTURE_3k0o\| PDB=3k0o \| SCENE= }}
-
	===Room temperature structure of CypA mutant Ser99Thr===		===Room temperature structure of CypA mutant Ser99Thr===
		+	{{ABSTRACT_PUBMED_19956261}}

-	~~{{ABSTRACT_PUBMED_019956261}}~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN]] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

	==About this Structure==		==About this Structure==
	[[3k0o]] 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=3K0O OCA].		[[3k0o]] 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=3K0O OCA].
-
-	==See Also==
-	*[[Cyclophilin\|Cyclophilin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019956261</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019956261</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]

OCA at 06:48, 20 October 2012

OCA — Sat, 20 Oct 2012 06:48:31 GMT

←Older revision		Revision as of 06:48, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3k0o]] is a 1 chain structure ~~of [[Cyclophilin]]~~ 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=3K0O OCA].	+	[[3k0o]] 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=3K0O OCA].

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

OCA at 14:21, 25 July 2012

OCA — Wed, 25 Jul 2012 14:21:35 GMT

←Older revision		Revision as of 14:21, 25 July 2012
Line 1:		Line 1:
	[[Image:3k0o.png\|left\|200px]]		[[Image:3k0o.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3k0o", 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_3k0o\| PDB=3k0o \| SCENE= }}		{{STRUCTURE_3k0o\| PDB=3k0o \| SCENE= }}

	===Room temperature structure of CypA mutant Ser99Thr===		===Room temperature structure of CypA mutant Ser99Thr===

		+	{{ABSTRACT_PUBMED_019956261}}

	==About this Structure==		==About this Structure==
Line 16:		Line 11:

	==See Also==		==See Also==
-	*[[Cyclophilin]]	+	*[[Cyclophilin\|Cyclophilin]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:019956261</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Alber, T.]]		[[Category: Alber, T.]]
	[[Category: Fraser, J S.]]		[[Category: Fraser, J S.]]
-	[[Category: Acetylation]]
	[[Category: Cyclosporin]]		[[Category: Cyclosporin]]
-	[[Category: Cytoplasm]]
	[[Category: Host-virus interaction]]		[[Category: Host-virus interaction]]
	[[Category: Isomerase]]		[[Category: Isomerase]]
Line 30:		Line 26:
	[[Category: Proline isomerase]]		[[Category: Proline isomerase]]
	[[Category: Rotamase]]		[[Category: Rotamase]]
-	[[Category: Ubl conjugation]]

OCA: Protected "3k0o" [edit=sysop:move=sysop]

OCA — Mon, 27 Dec 2010 01:49:45 GMT

Protected "3k0o" [edit=sysop:move=sysop]

←Older revision

Revision as of 01:49, 27 December 2010