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1eix

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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=1eix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eix OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eix RCSB], [http://www.ebi.ac.uk/pdbsum/1eix 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=1eix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1eix OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1eix RCSB], [http://www.ebi.ac.uk/pdbsum/1eix PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
 +
[[http://www.uniprot.org/uniprot/PYRF_ECOLI PYRF_ECOLI]] Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).[HAMAP-Rule:MF_01200_B]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 19:55, 24 December 2014

STRUCTURE OF OROTIDINE 5'-MONOPHOSPHATE DECARBOXYLASE FROM E. COLI, CO-CRYSTALLISED WITH THE INHIBITOR BMP

1eix, resolution 2.50Å

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