2l83

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</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=2l83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l83 RCSB], [http://www.ebi.ac.uk/pdbsum/2l83 PDBsum]</span></td></tr>
</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=2l83 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l83 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2l83 RCSB], [http://www.ebi.ac.uk/pdbsum/2l83 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/SAMP1_HALVD SAMP1_HALVD]] Protein modifier that is likely covalently attached to lysine residues of substrate proteins. The tagging system is termed SAMPylation. It is not known whether it is implicated in the targeting of proteins to the proteasome for degradation.
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</StructureSection>
</StructureSection>

Revision as of 11:04, 25 December 2014

A protein from Haloferax volcanii

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