2vwp: Difference between revisions

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<StructureSection load='2vwp' size='340' side='right'caption='[[2vwp]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
<StructureSection load='2vwp' size='340' side='right'caption='[[2vwp]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2vwp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_33500 Atcc 33500]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VWP FirstGlance]. <br>
<table><tr><td colspan='2'>[[2vwp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haloferax_mediterranei Haloferax mediterranei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VWP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VWP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.01&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2vwg|2vwg]], [[2b5w|2b5w]], [[2b5v|2b5v]], [[2vwh|2vwh]], [[2vwq|2vwq]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glucose_1-dehydrogenase Glucose 1-dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.47 1.1.1.47] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [https://pdbe.org/2vwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [https://www.ebi.ac.uk/pdbsum/2vwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vwp ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [https://pdbe.org/2vwp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [https://www.ebi.ac.uk/pdbsum/2vwp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vwp ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/GLCDH_HALMT GLCDH_HALMT]] Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-xylose, D-galactose, and D-fucose, to the corresponding glyconate. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a preference for NADP(+). Physiologically, seems to be involved in the degradation of glucose through a modified Entner-Doudoroff pathway.<ref>PMID:11425479</ref> <ref>PMID:8925901</ref>
[https://www.uniprot.org/uniprot/GLCDH_HALMT GLCDH_HALMT] Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate. Displays broad substrate specificity since it is able to catalyze the oxidation of a number of alternative aldose sugars, such as D-xylose, D-galactose, and D-fucose, to the corresponding glyconate. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a preference for NADP(+). Physiologically, seems to be involved in the degradation of glucose through a modified Entner-Doudoroff pathway.<ref>PMID:11425479</ref> <ref>PMID:8925901</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 33500]]
[[Category: Haloferax mediterranei]]
[[Category: Glucose 1-dehydrogenase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Baker, P J]]
[[Category: Baker PJ]]
[[Category: Bonete, M J]]
[[Category: Bonete MJ]]
[[Category: Britton, K L]]
[[Category: Britton KL]]
[[Category: Esclapez, J]]
[[Category: Esclapez J]]
[[Category: Ferrer, J]]
[[Category: Ferrer J]]
[[Category: Fisher, M]]
[[Category: Fisher M]]
[[Category: Pire, C]]
[[Category: Pire C]]
[[Category: Rice, D W]]
[[Category: Rice DW]]
[[Category: Alcohol dehydrogenase]]
[[Category: Glucose dehydrogenase]]
[[Category: Oxidoreductase]]
[[Category: Zinc dependent medium chain alcohol dehydrogenase family]]