5ok2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of the D10N mutant of beta-phosphoglucomutase from Lactococcus lactis inhibited with glucose 6-phosphate and tetrafluoroaluminate to 1.1A resolution.== | |
| - | + | <StructureSection load='5ok2' size='340' side='right' caption='[[5ok2]], [[Resolution|resolution]] 1.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5ok2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OK2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OK2 FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=BG6:BETA-D-GLUCOSE-6-PHOSPHATE'>BG6</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | |
| - | [[Category: | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.6 5.4.2.6] </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=5ok2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ok2 OCA], [http://pdbe.org/5ok2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ok2 RCSB], [http://www.ebi.ac.uk/pdbsum/5ok2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ok2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PGMB_LACLA PGMB_LACLA]] Catalyzes the interconversion of D-glucose 1-phosphate (G1P) and D-glucose 6-phosphate (G6P), 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. Glucose or lactose are used in preference to maltose, which is only utilized after glucose or lactose has been exhausted. It plays a key role in the regulation of the flow of carbohydrate intermediates in glycolysis and the formation of the sugar nucleotide UDP-glucose.<ref>PMID:9084169</ref> <ref>PMID:15005616</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Beta-phosphoglucomutase]] | ||
| + | [[Category: Bisson, C]] | ||
| + | [[Category: Robertson, A J]] | ||
| + | [[Category: General acid-base catalysis]] | ||
| + | [[Category: Isomerase]] | ||
| + | [[Category: Phosphoglucomutase]] | ||
| + | [[Category: Transition-state analogue]] | ||
Revision as of 07:15, 29 August 2018
Structure of the D10N mutant of beta-phosphoglucomutase from Lactococcus lactis inhibited with glucose 6-phosphate and tetrafluoroaluminate to 1.1A resolution.
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