5jhe

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Current revision (18:52, 20 September 2023) (edit) (undo)
 
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<StructureSection load='5jhe' size='340' side='right'caption='[[5jhe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='5jhe' size='340' side='right'caption='[[5jhe]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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 [http://proteopedia.org/fgij/fg.htm?mol=5JHE FirstGlance]. <br>
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<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>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5jhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jhe OCA], [http://pdbe.org/5jhe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jhe RCSB], [http://www.ebi.ac.uk/pdbsum/5jhe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jhe ProSAT]</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=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 ==
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[[http://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).
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[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==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Xu, L]]
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[[Category: Xu L]]
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[[Category: Yu, Q]]
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[[Category: Yu Q]]
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[[Category: Chaperone]]
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[[Category: Cochaperone]]
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Current revision

The Crystal Structure of the Saccharomyces cerevisiae Co-Chaperone Cpr7

PDB ID 5jhe

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