1e8k: Difference between revisions
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== | ==Cyclophilin 3 Complexed With Dipeptide Ala-Pro== | ||
<StructureSection load='1e8k' size='340' side='right'caption='[[1e8k]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<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='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='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'>[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> | |||
== 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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e8/1e8k_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e8k ConSurf]. | |||
<div style="clear:both"></div> | |||
== | ==See Also== | ||
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Caenorhabditis elegans]] | [[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]] | ||
Latest revision as of 14:56, 13 December 2023
Cyclophilin 3 Complexed With Dipeptide Ala-ProCyclophilin 3 Complexed With Dipeptide Ala-Pro
Structural highlights
FunctionCYP3_CAEEL PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also |
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