3p2l

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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=3p2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p2l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p2l RCSB], [http://www.ebi.ac.uk/pdbsum/3p2l 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=3p2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p2l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p2l RCSB], [http://www.ebi.ac.uk/pdbsum/3p2l PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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==See Also==
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[[http://www.uniprot.org/uniprot/CLPP_FRATT CLPP_FRATT]] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.[HAMAP-Rule:MF_00444]
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*[[Clp Protease|Clp Protease]]
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</StructureSection>
</StructureSection>

Revision as of 22:25, 24 December 2014

Crystal Structure of ATP-dependent Clp protease subunit P from Francisella tularensis

3p2l, resolution 2.29Å

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