3s6m
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 3s6m is ON HOLD Authors: Seattle Structural Genomics Center for Infectious Disease (SSGCID) Description: The structure of a Peptidyl-prolyl cis-tra...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The structure of a Peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei== |
| + | <StructureSection load='3s6m' size='340' side='right'caption='[[3s6m]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3s6m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_pseudomallei_1710b Burkholderia pseudomallei 1710b]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3S6M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3S6M 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]] 1.651Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=3s6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s6m OCA], [https://pdbe.org/3s6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3s6m RCSB], [https://www.ebi.ac.uk/pdbsum/3s6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3s6m ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q3JQT3_BURP1 Q3JQT3_BURP1] PPIases accelerate the folding of proteins (By similarity).[RuleBase:RU000493] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).[RuleBase:RU004223] | ||
| - | + | ==See Also== | |
| - | + | *[[Cyclophilin 3D structures|Cyclophilin 3D structures]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Burkholderia pseudomallei 1710b]] | ||
| + | [[Category: Large Structures]] | ||
Current revision
The structure of a Peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei
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