2ms4: Difference between revisions

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 ==Cyclophilin a complexed with a fragment of crk-ii==
-<StructureSection load='2ms4' size='340' side='right' caption='[[2ms4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2ms4' size='340' side='right'caption='[[2ms4]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ms4]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MS4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MS4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ms4]] is a 2 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=2MS4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MS4 FirstGlance]. <br>
-</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>
+</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='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=2ms4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ms4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ms4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ms4 PDBsum]</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=2ms4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ms4 OCA], [https://pdbe.org/2ms4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ms4 RCSB], [https://www.ebi.ac.uk/pdbsum/2ms4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ms4 ProSAT]</span></td></tr>
 </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.
+[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.
+==See Also==
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
 __TOC__
 </StructureSection>
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Homo sapiens]]
-[[Category: Jankowski, W]]
+[[Category: Large Structures]]
-[[Category: Kalodimos, C]]
+[[Category: Jankowski W]]
-[[Category: Rossi, P]]
+[[Category: Kalodimos C]]
-[[Category: Saleh, T]]
+[[Category: Rossi P]]
-[[Category: Cyclophilin some]]
+[[Category: Saleh T]]
-[[Category: Isomerase]]