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==Crystal structure of a peptidyl-prolyl cis-trans isomerase E (PPIE) from Homo sapiens at 2.50 A resolution== | |||
<StructureSection load='3uch' size='340' side='right'caption='[[3uch]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3uch]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UCH 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]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3uch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uch OCA], [https://pdbe.org/3uch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uch RCSB], [https://www.ebi.ac.uk/pdbsum/3uch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uch ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PPIE_HUMAN PPIE_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing. | |||
==See Also== | |||
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
Latest revision as of 11:11, 9 October 2024
Crystal structure of a peptidyl-prolyl cis-trans isomerase E (PPIE) from Homo sapiens at 2.50 A resolutionCrystal structure of a peptidyl-prolyl cis-trans isomerase E (PPIE) from Homo sapiens at 2.50 A resolution
Structural highlights
FunctionPPIE_HUMAN PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities. May be involved in muscle- and brain-specific processes. May be involved in pre-mRNA splicing. See Also |
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