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2m2a

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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=2m2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m2a RCSB], [http://www.ebi.ac.uk/pdbsum/2m2a 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=2m2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m2a RCSB], [http://www.ebi.ac.uk/pdbsum/2m2a PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/FKBX_ECOLI FKBX_ECOLI]] PPIases accelerate the folding of proteins. Substrate specificity investigated with 'Suc-Ala-Xaa-Pro-Phe-4-nitroanilide' where Xaa is the amino acid tested, was found to be Phe > Leu >> Ile > Lys = Ala > Trp > His >> Gln.
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</StructureSection>
</StructureSection>

Revision as of 09:52, 25 December 2014

NMR solution structure of the two domain PPIase SlpA from Escherichia coli

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