1xo7: Difference between revisions
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<StructureSection load='1xo7' size='340' side='right'caption='[[1xo7]], [[Resolution|resolution]] 1.61Å' scene=''> | <StructureSection load='1xo7' size='340' side='right'caption='[[1xo7]], [[Resolution|resolution]] 1.61Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xo7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1xo7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi Trypanosoma cruzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XO7 FirstGlance]. <br> | ||
</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=1xo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xo7 OCA], [https://pdbe.org/1xo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xo7 RCSB], [https://www.ebi.ac.uk/pdbsum/1xo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xo7 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.61Å</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=1xo7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xo7 OCA], [https://pdbe.org/1xo7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xo7 RCSB], [https://www.ebi.ac.uk/pdbsum/1xo7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xo7 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q4DPB9_TRYCC Q4DPB9_TRYCC] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Trypanosoma cruzi]] | ||
[[Category: Caruthers | [[Category: Caruthers JM]] | ||
[[Category: Hol | [[Category: Hol WGJ]] | ||
Latest revision as of 09:48, 23 August 2023
Crystal structure of cyclophilin from Trypanosoma cruziCrystal structure of cyclophilin from Trypanosoma cruzi
Structural highlights
FunctionQ4DPB9_TRYCC PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.[RuleBase:RU004223] 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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