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<table><tr><td colspan='2'>[[1ist]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IST FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ist]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IST 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='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> | ||
<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=1ist FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ist OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ist RCSB], [http://www.ebi.ac.uk/pdbsum/1ist PDBsum]</span></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=1ist FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ist OCA], [http://pdbe.org/1ist PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ist RCSB], [http://www.ebi.ac.uk/pdbsum/1ist PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
Revision as of 05:52, 10 September 2015
Crystal structure of yeast cyclophilin A, CPR1Crystal structure of yeast cyclophilin A, CPR1
Structural highlights
Function[CYPH_YEAST] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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