1qng - Revision history

OCA at 12:49, 13 December 2023

OCA — Wed, 13 Dec 2023 12:49:33 GMT

←Older revision		Revision as of 12:49, 13 December 2023
Line 3:		Line 3:
	<StructureSection load='1qng' size='340' side='right'caption='[[1qng]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1qng' size='340' side='right'caption='[[1qng]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qng]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Plafa Plafa~~] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qng]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QNG FirstGlance]. <br>
-	</td></tr><tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non~~-~~Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</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]] 2.1Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></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=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [https://pdbe.org/1qng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [https://www.ebi.ac.uk/pdbsum/1qng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qng 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=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [https://pdbe.org/1qng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [https://www.ebi.ac.uk/pdbsum/1qng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qng ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/Q25756_PLAFA Q25756_PLAFA]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223]	+	[https://www.uniprot.org/uniprot/Q25756_PLAFA Q25756_PLAFA] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223]
	== 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: ~~Peptidylprolyl isomerase]]~~	+	[[Category: Plasmodium falciparum]]
-	~~[[Category: Plafa~~]]	+
	[[Category: Tolypocladium inflatum]]		[[Category: Tolypocladium inflatum]]
-	[[Category: Hall~~, D R~~]]	+	[[Category: Hall DR]]
-	[[Category: Hunter~~, W N~~]]	+	[[Category: Hunter WN]]
-	[[Category: Peterson~~, M R]]~~	+	[[Category: Peterson MR]]
-	~~[[Category: Cyclophilin]]~~	+
-	~~[[Category: Cyclophilin-cyclosporin complex]]~~	+
-	~~[[Category: Cyclosporin some]]~~	+
-	~~[[Category: Immunosuppressant]]~~	+
-	~~[[Category: Isomerase-immunosuppressant complex~~]]	+

OCA at 09:55, 26 May 2021

OCA — Wed, 26 May 2021 09:55:08 GMT

←Older revision		Revision as of 09:55, 26 May 2021
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	<StructureSection load='1qng' size='340' side='right'caption='[[1qng]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1qng' size='340' side='right'caption='[[1qng]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1qng]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Plafa Plafa] and [~~http~~://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1QNG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1qng]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Plafa Plafa] and [https://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QNG FirstGlance]. <br>
	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>		</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</div></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=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [~~http~~://pdbe.org/1qng PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1qng PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1qng 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=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [https://pdbe.org/1qng PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [https://www.ebi.ac.uk/pdbsum/1qng PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qng ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/Q25756_PLAFA Q25756_PLAFA]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223]	+	[[https://www.uniprot.org/uniprot/Q25756_PLAFA Q25756_PLAFA]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 07:18, 21 August 2019

OCA — Wed, 21 Aug 2019 07:18:56 GMT

←Older revision		Revision as of 07:18, 21 August 2019
Line 1:		Line 1:

	==Plasmodium falciparum Cyclophilin complexed with Cyclosporin A==		==Plasmodium falciparum Cyclophilin complexed with Cyclosporin A==
-	<StructureSection load='1qng' size='340' side='right' caption='[[1qng]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='1qng' size='340' side='right'caption='[[1qng]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qng]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa] and [http://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QNG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qng]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa] and [http://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QNG FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/1qng_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qn/1qng_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 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1qng" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1qng" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Cyclophilin 3D structures\|Cyclophilin 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Plafa]]		[[Category: Plafa]]

OCA at 14:30, 15 November 2017

OCA — Wed, 15 Nov 2017 14:30:13 GMT

←Older revision		Revision as of 14:30, 15 November 2017
Line 1:		Line 1:
		+
	==Plasmodium falciparum Cyclophilin complexed with Cyclosporin A==		==Plasmodium falciparum Cyclophilin complexed with Cyclosporin A==
	<StructureSection load='1qng' size='340' side='right' caption='[[1qng]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='1qng' size='340' side='right' caption='[[1qng]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</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=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [http://pdbe.org/1qng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [http://www.ebi.ac.uk/pdbsum/1qng 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=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [http://pdbe.org/1qng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [http://www.ebi.ac.uk/pdbsum/1qng PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qng ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 29:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 1qng" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 1qng" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Cyclophilin\|Cyclophilin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:51, 10 February 2016

OCA — Wed, 10 Feb 2016 07:51:57 GMT

←Older revision		Revision as of 07:51, 10 February 2016
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	<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=1qng ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 06:52, 11 September 2015

OCA — Fri, 11 Sep 2015 06:52:14 GMT

←Older revision		Revision as of 06:52, 11 September 2015
Line 6:		Line 6:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</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=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [http://www.ebi.ac.uk/pdbsum/1qng 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=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [http://pdbe.org/1qng PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [http://www.ebi.ac.uk/pdbsum/1qng 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 1qng" style="background-color:#fffaf0;"></div>

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

OCA at 12:50, 25 December 2014

OCA — Thu, 25 Dec 2014 12:50:09 GMT

←Older revision		Revision as of 12:50, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1qng]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa] and [http://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QNG FirstGlance]. <br>		<table><tr><td colspan='2'>[[1qng]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa] and [http://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QNG FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>	+	</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [http://www.ebi.ac.uk/pdbsum/1qng 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=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [http://www.ebi.ac.uk/pdbsum/1qng PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/Q25756_PLAFA Q25756_PLAFA]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 36:		Line 38:
	[[Category: Plafa]]		[[Category: Plafa]]
	[[Category: Tolypocladium inflatum]]		[[Category: Tolypocladium inflatum]]
-	[[Category: Hall, D R.]]	+	[[Category: Hall, D R]]
-	[[Category: Hunter, W N.]]	+	[[Category: Hunter, W N]]
-	[[Category: Peterson, M R.]]	+	[[Category: Peterson, M R]]
	[[Category: Cyclophilin]]		[[Category: Cyclophilin]]
	[[Category: Cyclophilin-cyclosporin complex]]		[[Category: Cyclophilin-cyclosporin complex]]

OCA at 09:52, 3 October 2014

OCA — Fri, 03 Oct 2014 09:52:30 GMT

←Older revision		Revision as of 09:52, 3 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1qng~~\| ~~PDB~~=1qng \| ~~SCENE~~= }}	+	==Plasmodium falciparum Cyclophilin complexed with Cyclosporin A==
-	===Plasmodium falciparum ~~Cyclophilin~~ complexed with ~~Cyclosporin~~ A===	+	<StructureSection load='1qng' size='340' side='right' caption='[[1qng]], [[Resolution\|resolution]] 2.10Å' scene=''>
-	~~{{ABSTRACT_PUBMED_10756109}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1qng]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa] and [http://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QNG FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</scene>, <scene name='pdbligand=BMT:4-METHYL-4-[(E)-2-BUTENYL]-4,N-METHYL-THREONINE'>BMT</scene>, <scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene>, <scene name='pdbligand=MVA:N-METHYLVALINE'>MVA</scene>, <scene name='pdbligand=SAR:SARCOSINE'>SAR</scene></td></tr>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1bck\|1bck]], [[1c5f\|1c5f]], [[1csa\|1csa]], [[1cwa\|1cwa]], [[1cwb\|1cwb]], [[1cwc\|1cwc]], [[1cwf\|1cwf]], [[1cwh\|1cwh]], [[1cwi\|1cwi]], [[1cwj\|1cwj]], [[1cwk\|1cwk]], [[1cwl\|1cwl]], [[1cwm\|1cwm]], [[1cwo\|1cwo]], [[1cya\|1cya]], [[1cyb\|1cyb]], [[1cyn\|1cyn]], [[1ikf\|1ikf]], [[1m63\|1m63]], [[1mf8\|1mf8]], [[1mik\|1mik]], [[1qnh\|1qnh]], [[1xq7\|1xq7]], [[2esl\|2esl]], [[2oju\|2oju]], [[2poy\|2poy]], [[2rma\|2rma]], [[2rmb\|2rmb]], [[2rmc\|2rmc]], [[2wfj\|2wfj]], [[2x2c\|2x2c]], [[2x7k\|2x7k]], [[2z6w\|2z6w]], [[3bo7\|3bo7]], [[3cys\|3cys]], [[3eov\|3eov]]</td></tr>
		+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qng FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qng OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qng RCSB], [http://www.ebi.ac.uk/pdbsum/1qng 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/qn/1qng_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 ==
		+	Cyclosporin A (CsA) is a potent anti-malarial compound in vitro and in vivo in mice though better known for its immunosuppressive properties in humans. Crystal structures of wild-type and a double mutant Plasmodium falciparum cyclophilin (PfCyP19 and mPfCyP19) complexed with CsA have been determined using diffraction terms to a resolution of 2.1 A (1 A=0.1 nm). The wild-type has a single PfCyP19/CsA complex per asymmetric unit in space group P1 and refined to an R-work of 0.15 and R-free of 0.19. An altered cyclophilin, with two accidental mutations, Phe120 to Leu in the CsA binding pocket and Leu171 to Trp at the C terminus, presents two complexes per asymmetric unit in the orthorhombic space group P2(1)2(1)2. This refined to an R-work of 0.18 and R-free 0.21. The mutations were identified from the crystallographic analysis and the C-terminal alteration helps to explain the different crystal forms obtained. PfCyP19 shares approximately 61 % sequence identity with human cyclophilin A (hCyPA) and the structures are similar, consisting of an eight-stranded antiparallel beta-barrel core capped by two alpha-helices. The fold creates a hydrophobic active-site, the floor of which is formed by side-chains of residues from four antiparallel beta-strands and the walls from loops and turns. We identified C-H.O hydrogen bonds between the drug and protein that may be an important feature of cyclophilins and suggest a general mode of interaction between hydrophobic molecules. Comparisons with cyclophilin-dipeptide complexes suggests that a specific C-H.O hydrogen bonding interaction may contribute to ligand binding. Residues Ser106, His99 and Asp130, located close to the active site and conserved in most cyclophilins, are arranged in a manner reminiscent of a serine protease catalytic triad. A Ser106Ala mutant was engineered to test the hypothesis that this triad contributes to CyP function. Mutant and wild-type enzymes were found to have similar catalytic properties.

-	~~==Function==~~	+	The three-dimensional structure of a Plasmodium falciparum cyclophilin in complex with the potent anti-malarial cyclosporin A.,Peterson MR, Hall DR, Berriman M, Nunes JA, Leonard GA, Fairlamb AH, Hunter WN J Mol Biol. 2000 Apr 21;298(1):123-33. PMID:10756109<ref>PMID:10756109</ref>
-	~~[[http://www~~.~~uniprot~~.~~org/uniprot/Q25756_PLAFA Q25756_PLAFA]] PPIases accelerate the folding of proteins~~ (~~By similarity~~)~~.[RuleBase~~:~~RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis~~-~~trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity)~~.~~[RuleBase~~:~~RU004223]~~	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[1qng]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Plafa Plafa] and [http://en~~.~~wikipedia.org~~/~~wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA].~~	+	</div>

	==See Also==		==See Also==
	*[[Cyclophilin\|Cyclophilin]]		*[[Cyclophilin\|Cyclophilin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:010756109</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Plafa]]		[[Category: Plafa]]

OCA at 13:38, 12 March 2014

OCA — Wed, 12 Mar 2014 13:38:28 GMT

←Older revision		Revision as of 13:38, 12 March 2014
Line 1:		Line 1:
-	[[Image:1qng.png\|left\|200px]]
-
	{{STRUCTURE_1qng\| PDB=1qng \| SCENE= }}		{{STRUCTURE_1qng\| PDB=1qng \| SCENE= }}
-
	===Plasmodium falciparum Cyclophilin complexed with Cyclosporin A===		===Plasmodium falciparum Cyclophilin complexed with Cyclosporin A===
		+	{{ABSTRACT_PUBMED_10756109}}

-	~~{{ABSTRACT_PUBMED_10756109}}~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/Q25756_PLAFA Q25756_PLAFA]] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223]

	==About this Structure==		==About this Structure==
-	[[1qng]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Plasmodium_falciparum Plasmodium falciparum~~] and [http://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA].	+	[[1qng]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plafa Plafa] and [http://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA].

	==See Also==		==See Also==
Line 14:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:010756109</ref><~~ref~~ group="xtra"~~>PMID:009716503<~~/~~ref~~><references ~~group="xtra"~~/>	+	<ref group="xtra">PMID:010756109</ref><references group="xtra"/><references/>
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
-	[[Category: ~~Plasmodium falciparum~~]]	+	[[Category: Plafa]]
	[[Category: Tolypocladium inflatum]]		[[Category: Tolypocladium inflatum]]
	[[Category: Hall, D R.]]		[[Category: Hall, D R.]]

OCA at 16:52, 20 October 2012

OCA — Sat, 20 Oct 2012 16:52:23 GMT

←Older revision		Revision as of 16:52, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1qng]] is a 2 chain structure ~~of [[Cyclophilin]]~~ with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] and [http://en.wikipedia.org/wiki/~~Tolypocladium_inflatum_gams~~ Tolypocladium inflatum ~~gams~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA].	+	[[1qng]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum] and [http://en.wikipedia.org/wiki/Tolypocladium_inflatum Tolypocladium inflatum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNG OCA].

	==See Also==		==See Also==
Line 17:		Line 17:
	[[Category: Peptidylprolyl isomerase]]		[[Category: Peptidylprolyl isomerase]]
	[[Category: Plasmodium falciparum]]		[[Category: Plasmodium falciparum]]
-	[[Category: Tolypocladium inflatum ~~gams~~]]	+	[[Category: Tolypocladium inflatum]]
	[[Category: Hall, D R.]]		[[Category: Hall, D R.]]
	[[Category: Hunter, W N.]]		[[Category: Hunter, W N.]]