4nuw

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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=4nuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nuw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nuw RCSB], [http://www.ebi.ac.uk/pdbsum/4nuw 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=4nuw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nuw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nuw RCSB], [http://www.ebi.ac.uk/pdbsum/4nuw 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 01:40, 25 December 2014

Crystal structure of orotidine 5'-monophosphate decarboxylase from methanobacterium thermoautotrophicum complexed with uridine 5'-monophosphate

4nuw, resolution 1.59Å

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