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2b5v

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==Crystal structure of glucose dehydrogenase from Haloferax mediterranei==
==Crystal structure of glucose dehydrogenase from Haloferax mediterranei==
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<StructureSection load='2b5v' size='340' side='right' caption='[[2b5v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='2b5v' size='340' side='right'caption='[[2b5v]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2b5v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33500 Atcc 33500]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2B5V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2b5v]] 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=2B5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b5w|2b5w]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b5w|2b5w]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gdh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2252 ATCC 33500])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gdh ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2252 ATCC 33500])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose_1-dehydrogenase Glucose 1-dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.47 1.1.1.47] </span></td></tr>
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<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>
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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=2b5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5v OCA], [http://pdbe.org/2b5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2b5v RCSB], [http://www.ebi.ac.uk/pdbsum/2b5v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5v ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5v OCA], [https://pdbe.org/2b5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5v RCSB], [https://www.ebi.ac.uk/pdbsum/2b5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5v ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[[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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[[Category: Atcc 33500]]
[[Category: Atcc 33500]]
[[Category: Glucose 1-dehydrogenase]]
[[Category: Glucose 1-dehydrogenase]]
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[[Category: Large Structures]]
[[Category: Baker, P J]]
[[Category: Baker, P J]]
[[Category: Bonete, M J]]
[[Category: Bonete, M J]]

Revision as of 11:36, 3 February 2021

Crystal structure of glucose dehydrogenase from Haloferax mediterranei

PDB ID 2b5v

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