4s1e: Difference between revisions
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==Crystal structure of cyclophilin mutant L120A from Leishmania donovani at 2.22 angstrom.== | ==Crystal structure of cyclophilin mutant L120A from Leishmania donovani at 2.22 angstrom.== | ||
<StructureSection load='4s1e' size='340' side='right' caption='[[4s1e]], [[Resolution|resolution]] 2.22Å' scene=''> | <StructureSection load='4s1e' size='340' side='right'caption='[[4s1e]], [[Resolution|resolution]] 2.22Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4s1e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S1E OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4s1e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_donovani Leishmania donovani]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S1E 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]] 2.22Å</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=4s1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s1e OCA], [https://pdbe.org/4s1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s1e RCSB], [https://www.ebi.ac.uk/pdbsum/4s1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s1e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/Q9U9R3_LEIDO Q9U9R3_LEIDO] PPIases accelerate the folding of proteins.[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] | ||
==See Also== | ==See Also== | ||
*[[Peptidyl-prolyl cis-trans isomerase|Peptidyl-prolyl cis-trans isomerase]] | *[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]] | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Leishmania donovani]] | ||
[[Category: | [[Category: Banerjee R]] | ||
[[Category: | [[Category: Datta AK]] | ||
[[Category: | [[Category: Roy S]] | ||
Latest revision as of 18:00, 20 September 2023
Crystal structure of cyclophilin mutant L120A from Leishmania donovani at 2.22 angstrom.
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