1e8k
From Proteopedia
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==Cyclophilin 3 Complexed With Dipeptide Ala-Pro== | ==Cyclophilin 3 Complexed With Dipeptide Ala-Pro== | ||
| - | <StructureSection load='1e8k' size='340' side='right' caption='[[1e8k]], [[Resolution|resolution]] 1.90Å' scene=''> | + | <StructureSection load='1e8k' size='340' side='right'caption='[[1e8k]], [[Resolution|resolution]] 1.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1e8k]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1e8k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E8K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E8K 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]] 1.9Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></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=1e8k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e8k OCA], [https://pdbe.org/1e8k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e8k RCSB], [https://www.ebi.ac.uk/pdbsum/1e8k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e8k ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [ | + | [https://www.uniprot.org/uniprot/CYP3_CAEEL CYP3_CAEEL] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Cyclophilin|Cyclophilin]] | + | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Caenorhabditis elegans]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Dornan | + | [[Category: Dornan J]] |
| - | [[Category: Kontopidis | + | [[Category: Kontopidis G]] |
| - | [[Category: Taylor | + | [[Category: Taylor P]] |
| - | [[Category: Walkinshaw | + | [[Category: Walkinshaw MD]] |
| - | [[Category: Wu | + | [[Category: Wu SY]] |
| - | + | ||
Current revision
Cyclophilin 3 Complexed With Dipeptide Ala-Pro
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