5ojz
From Proteopedia
(Difference between revisions)
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==D10N variant of beta-phosphoglucomutase from Lactococcus lactis inhibited by a beryllium triflouride phosphoenzyme analogue to 1.3A resolution.== | ==D10N variant of beta-phosphoglucomutase from Lactococcus lactis inhibited by a beryllium triflouride phosphoenzyme analogue to 1.3A resolution.== | ||
| - | <StructureSection load='5ojz' size='340' side='right' caption='[[5ojz]], [[Resolution|resolution]] 1.30Å' scene=''> | + | <StructureSection load='5ojz' size='340' side='right'caption='[[5ojz]], [[Resolution|resolution]] 1.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5ojz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OJZ OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[5ojz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OJZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5OJZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
<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='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:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5ojz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ojz OCA], [http://pdbe.org/5ojz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ojz RCSB], [http://www.ebi.ac.uk/pdbsum/5ojz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ojz ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == 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> | [[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> | ||
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| + | ==See Also== | ||
| + | *[[Beta-phosphoglucomutase 3D structures|Beta-phosphoglucomutase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Beta-phosphoglucomutase]] | [[Category: Beta-phosphoglucomutase]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Bisson, C]] | [[Category: Bisson, C]] | ||
[[Category: Robertson, A J]] | [[Category: Robertson, A J]] | ||
Revision as of 12:24, 26 August 2020
D10N variant of beta-phosphoglucomutase from Lactococcus lactis inhibited by a beryllium triflouride phosphoenzyme analogue to 1.3A resolution.
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