1oca: Difference between revisions

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==HUMAN CYCLOPHILIN A, UNLIGATED, NMR, 20 STRUCTURES==

== Structural highlights ==

<table><tr><td colspan='2'>[[1oca]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCA OCA]. For a guided tour on the structure components use [https://proteopedia.org/fgij/fg.htm?mol=1OCA FirstGlance].

<table><tr><td colspan='2'>[[1oca]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCA OCA]. For a guided tour on the structure components use [https://proteopedia.org/fgij/fg.htm?mol=1OCA FirstGlance].

</td></tr><tr id='~~gene~~'><td class="sblockLbl">[[~~Gene~~|~~Gene~~:]]</td><td class="sblockDat"~~>CYCLOPHILIN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~

</td></tr><tr id='method'><td class="sblockLbl">[[Empirical_models|Method:]]</td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>

~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~">Activity:</td><td class="sblockDat">[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] </td></tr>

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[https://proteopedia.org/fgij/fg.htm?mol=1oca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oca OCA], [https://pdbe.org/1oca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oca RCSB], [https://www.ebi.ac.uk/pdbsum/1oca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oca ProSAT]</td></tr>

</table>

== 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 ==

[[Image:Consurf_key_small.gif|200px|right]]

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__TOC__

</StructureSection>

[[Category: ~~Human~~]]

[[Category: Homo sapiens]]

[[Category: Large Structures]]

~~[[Category: Peptidylprolyl isomerase]]~~

[[Category: Guntert P]]

[[Category: Guntert, P]]

[[Category: Ottiger M]]

[[Category: Ottiger, M]]

[[Category: Wuthrich K]]

[[Category: Wuthrich, K]]

[[Category: Zerbe O]]

[[Category: Zerbe, O]]

~~[[Category: Isomerase]]~~

~~[[Category: Peptidyl-prolyl cis-trans isomerase~~]]

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@@ Line 1: / Line 1: @@
 ==HUMAN CYCLOPHILIN A, UNLIGATED, NMR, 20 STRUCTURES==
-<StructureSection load='1oca' size='340' side='right'caption='[[1oca]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1oca' size='340' side='right'caption='[[1oca]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1oca]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OCA FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1oca]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OCA FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYCLOPHILIN ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1oca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oca OCA], [https://pdbe.org/1oca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oca RCSB], [https://www.ebi.ac.uk/pdbsum/1oca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oca ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Guntert P]]
-[[Category: Guntert, P]]
+[[Category: Ottiger M]]
-[[Category: Ottiger, M]]
+[[Category: Wuthrich K]]
-[[Category: Wuthrich, K]]
+[[Category: Zerbe O]]
-[[Category: Zerbe, O]]
-[[Category: Isomerase]]
-[[Category: Peptidyl-prolyl cis-trans isomerase]]