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5jhe
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==The Crystal Structure of the Saccharomyces cerevisiae Co-Chaperone Cpr7== | ==The Crystal Structure of the Saccharomyces cerevisiae Co-Chaperone Cpr7== | ||
| - | <StructureSection load='5jhe' size='340' side='right' caption='[[5jhe]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='5jhe' size='340' side='right'caption='[[5jhe]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5jhe]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JHE OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[5jhe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JHE 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">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jhe OCA], [https://pdbe.org/5jhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jhe RCSB], [https://www.ebi.ac.uk/pdbsum/5jhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jhe ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CYP7_YEAST CYP7_YEAST] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Plays a major role in negative regulation of the heat shock transcription factor (HSF). |
| + | |||
| + | ==See Also== | ||
| + | *[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: | + | [[Category: Xu L]] |
| - | [[Category: | + | [[Category: Yu Q]] |
| - | + | ||
Current revision
The Crystal Structure of the Saccharomyces cerevisiae Co-Chaperone Cpr7
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