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1dka

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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=1dka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dka OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dka RCSB], [http://www.ebi.ac.uk/pdbsum/1dka 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=1dka FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dka OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dka RCSB], [http://www.ebi.ac.uk/pdbsum/1dka PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/DGDA_BURCE DGDA_BURCE]] The dialkylglycine decarboxylase is of interest because it normally catalyzes both decarboxylation and amino transfer. It may be more properly described as a decarboxylating aminotransferase rather than an aminotransferring decarboxylase.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 05:50, 25 December 2014

DIALKYLGLYCINE DECARBOXYLASE STRUCTURE: BIFUNCTIONAL ACTIVE SITE AND ALKALI METAL BINDING SITES

1dka, resolution 2.60Å

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