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1vdn
From Proteopedia
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<StructureSection load='1vdn' size='340' side='right'caption='[[1vdn]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='1vdn' size='340' side='right'caption='[[1vdn]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1vdn]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1vdn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VDN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VDN 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]] 1.6Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=MCM:7-AMINO-4-METHYL-CHROMEN-2-ONE'>MCM</scene></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=1vdn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vdn OCA], [https://pdbe.org/1vdn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vdn RCSB], [https://www.ebi.ac.uk/pdbsum/1vdn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vdn ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CYPH_YEAST 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.<ref>PMID:11641409</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Konno | + | [[Category: Konno M]] |
| - | [[Category: Okudaira | + | [[Category: Okudaira K]] |
| - | [[Category: Shibano | + | [[Category: Shibano T]] |
| - | [[Category: Takahashi | + | [[Category: Takahashi N]] |
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Current revision
Crystal Structure Of Yeast Cyclophilin A Complexed With ACE-Ala-Ala-Pro-Ala-7-Amino-4-Methylcoumarin
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