2n0t: Difference between revisions
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==Structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution== | ==Structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution== | ||
<StructureSection load='2n0t' size='340' side='right'caption='[[2n0t | <StructureSection load='2n0t' size='340' side='right'caption='[[2n0t]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2n0t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2n0t]] 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=2N0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N0T FirstGlance]. <br> | ||
</td></tr><tr id=' | </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'>[https://proteopedia.org/fgij/fg.htm?mol=2n0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0t OCA], [https://pdbe.org/2n0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n0t RCSB], [https://www.ebi.ac.uk/pdbsum/2n0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0t 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=2n0t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n0t OCA], [https://pdbe.org/2n0t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n0t RCSB], [https://www.ebi.ac.uk/pdbsum/2n0t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n0t 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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bibow S]] | |||
[[Category: Bibow | [[Category: Chi CN]] | ||
[[Category: Chi | [[Category: Guntert P]] | ||
[[Category: Guntert | [[Category: Orts J]] | ||
[[Category: Orts | [[Category: Riek R]] | ||
[[Category: Riek | [[Category: Strotz D]] | ||
[[Category: Strotz | [[Category: Voegeli B]] | ||
[[Category: Voegeli | |||
Latest revision as of 06:13, 15 May 2024
Structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution
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