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3s6m

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3s6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s6m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s6m RCSB], [http://www.ebi.ac.uk/pdbsum/3s6m PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3s6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3s6m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3s6m RCSB], [http://www.ebi.ac.uk/pdbsum/3s6m PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://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]
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</StructureSection>
</StructureSection>

Revision as of 11:20, 25 December 2014

The structure of a Peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei

3s6m, resolution 1.65Å

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