This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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...) |
|||
| (8 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''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
| |||||||||||
