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4o29

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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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [http://www.ebi.ac.uk/pdbsum/4o29 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=4o29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4o29 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4o29 RCSB], [http://www.ebi.ac.uk/pdbsum/4o29 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PIMT_PYRAE PIMT_PYRAE]] Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
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</StructureSection>
</StructureSection>

Revision as of 03:57, 25 December 2014

PROTEIN-L-ISOASPARTATE O-METHYLTRANSFERASE from Pyrobaculum aerophilum in COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE

4o29, resolution 2.90Å

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