2m2a: Difference between revisions

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'''Unreleased structure'''


The entry 2m2a is ON HOLD
==NMR solution structure of the two domain PPIase SlpA from Escherichia coli==
<StructureSection load='2m2a' size='340' side='right'caption='[[2m2a]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m2a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M2A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M2A FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2m2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m2a OCA], [https://pdbe.org/2m2a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m2a RCSB], [https://www.ebi.ac.uk/pdbsum/2m2a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m2a ProSAT]</span></td></tr>
</table>
== Function ==
[https://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.


Authors: Kovermann, M., Weininger, U., Balbach, J.
==See Also==
 
*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
Description: NMR solution structure of the two domain PPIase SlpA from Escherichia coli
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Balbach J]]
[[Category: Kovermann M]]
[[Category: Weininger U]]

Latest revision as of 05:58, 15 May 2024

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

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