1lp6

<table><tr><td colspan='2'>[[1lp6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"archaea"_woese_et_al._1990 "archaea" woese et al. 1990]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LP6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LP6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C5P:CYTIDINE-5-MONOPHOSPHATE'>C5P</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1lol|1lol]], [[1loq|1loq]], [[1lor|1lor]], [[1los|1los]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Orotidine-5'-phosphate_decarboxylase Orotidine-5'-phosphate decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.23 4.1.1.23] </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=1lp6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lp6 OCA], [http://pdbe.org/1lp6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lp6 RCSB], [http://www.ebi.ac.uk/pdbsum/1lp6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lp6 ProSAT]</span></td></tr>

[[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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== Publication Abstract from PubMed ==

The crystal structures of the enzyme orotidine-5'-monophosphate decarboxylase from Methanobacterium thermoautotrophicum complexed with its product UMP and the inhibitors 6-hydroxyuridine 5'-phosphate (BMP), XMP, and CMP are reported. A mutant version of the protein, in which four residues of the flexible phosphate-binding loop (180)Gly-Gly(190) were removed and Arg(203) was replaced by alanine, was also analyzed. The XMP and CMP complexes reveal a ligand-binding mode that is distinct from the one identified previously with the aromatic rings located outside the binding pocket. A potential pathway for ligand binding is discussed.

Crystal structures of inhibitor complexes reveal an alternate binding mode in orotidine-5'-monophosphate decarboxylase.,Wu N, Pai EF J Biol Chem. 2002 Aug 2;277(31):28080-7. Epub 2002 May 13. PMID:12011084<ref>PMID:12011084</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1lp6" style="background-color:#fffaf0;"></div>

*[[Uridine 5'-monophosphate synthase|Uridine 5'-monophosphate synthase]]

[[Category: Archaea woese et al. 1990]]

[[Category: Pai, E F]]

[[Category: Wu, N]]

[[Category: Tim barrel]]