2n0t

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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==
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<StructureSection load='2n0t' size='340' side='right'caption='[[2n0t]], [[NMR_Ensembles_of_Models | 40 NMR models]]' scene=''>
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<StructureSection load='2n0t' size='340' side='right'caption='[[2n0t]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2n0t]] 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=2N0T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N0T FirstGlance]. <br>
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<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>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mzu|2mzu]]</div></td></tr>
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</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>
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<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>
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<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>
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<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>
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</table>
</table>
== Function ==
== Function ==
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[[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.
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[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>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Bibow S]]
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[[Category: Bibow, S]]
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[[Category: Chi CN]]
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[[Category: Chi, C N]]
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[[Category: Guntert P]]
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[[Category: Guntert, P]]
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[[Category: Orts J]]
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[[Category: Orts, J]]
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[[Category: Riek R]]
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[[Category: Riek, R]]
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[[Category: Strotz D]]
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[[Category: Strotz, D]]
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[[Category: Voegeli B]]
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[[Category: Voegeli, B]]
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[[Category: Isomerase]]
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Revision as of 08:13, 8 March 2023

Structural ensemble of the enzyme cyclophilin reveals an orchestrated mode of action at atomic resolution

PDB ID 2n0t

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