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< | ==CYCLOPHILIN 3 complexed with DIPEPTIDE GLY-PRO== | ||
<StructureSection load='2igw' size='340' side='right'caption='[[2igw]], [[Resolution|resolution]] 1.78Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2igw]] 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=2IGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IGW 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]] 1.78Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</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=2igw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2igw OCA], [https://pdbe.org/2igw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2igw RCSB], [https://www.ebi.ac.uk/pdbsum/2igw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2igw 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/ig/2igw_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=2igw 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: Kan | [[Category: Kan D]] | ||
Latest revision as of 13:10, 30 August 2023
CYCLOPHILIN 3 complexed with DIPEPTIDE GLY-PROCYCLOPHILIN 3 complexed with DIPEPTIDE GLY-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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