4lc6

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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=4lc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lc6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lc6 RCSB], [http://www.ebi.ac.uk/pdbsum/4lc6 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=4lc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lc6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lc6 RCSB], [http://www.ebi.ac.uk/pdbsum/4lc6 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/PYRF_METTH PYRF_METTH]] Catalyzes the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP).[HAMAP-Rule:MF_01200_A]
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</StructureSection>
</StructureSection>

Revision as of 17:28, 24 December 2014

Crystal structure of the mutant H128Q of orotidine 5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum complexed with the inhibitor BMP

4lc6, resolution 1.32Å

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