3nas

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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=3nas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nas RCSB], [http://www.ebi.ac.uk/pdbsum/3nas 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=3nas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nas OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nas RCSB], [http://www.ebi.ac.uk/pdbsum/3nas PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/PGMB_BACSU PGMB_BACSU]] Catalyze the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), and forming beta-D-glucose 1,6-(bis)phosphate (beta-G16P) as an intermediate. The beta-phosphoglucomutase (Beta-PGM) acts on the beta-C(1) anomer of G1P. It play a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 18:29, 25 December 2014

The crystal structure of beta-phosphoglucomutase from Bacillus subtilis

3nas, resolution 3.00Å

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