2vwp - Revision history

OCA at 15:35, 13 December 2023

2023-12-13T15:35:14Z

← Older revision		Revision as of 15:35, 13 December 2023
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	<StructureSection load='2vwp' size='340' side='right'caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='2vwp' size='340' side='right'caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' 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]] 2.01Å</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~~]]

OCA at 10:49, 7 July 2021

2021-07-07T10:49:59Z

← Older revision		Revision as of 10:49, 7 July 2021
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	<StructureSection load='2vwp' size='340' side='right'caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='2vwp' size='340' side='right'caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vwp]] 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=2VWP OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/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/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>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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='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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vwg\|2vwg]], [[2b5w\|2b5w]], [[2b5v\|2b5v]], [[2vwh\|2vwh]], [[2vwq\|2vwq]]</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='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>		<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'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [~~http~~://pdbe.org/2vwp PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2vwp PDBsum], [~~http~~://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 ==
	[[~~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>		[[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]]

OCA at 07:17, 10 July 2019

2019-07-10T07:17:11Z

← Older revision		Revision as of 07:17, 10 July 2019
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	==Haloferax mediterranei glucose dehydrogenase in complex with NADPH and Zn.==		==Haloferax mediterranei glucose dehydrogenase in complex with NADPH and Zn.==
	<StructureSection load='2vwp' size='340' side='right' caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='2vwp' size='340' side='right'caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vwp]] 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=2VWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VWP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vwp]] 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=2VWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VWP FirstGlance]. <br>
Line 15:		Line 15:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vw/2vwp_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vw/2vwp_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
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	[[Category: Atcc 33500]]		[[Category: Atcc 33500]]
	[[Category: Glucose 1-dehydrogenase]]		[[Category: Glucose 1-dehydrogenase]]
			[[Category: Large Structures]]
	[[Category: Baker, P J]]		[[Category: Baker, P J]]
	[[Category: Bonete, M J]]		[[Category: Bonete, M J]]

OCA at 11:21, 7 October 2017

2017-10-07T11:21:45Z

← Older revision		Revision as of 11:21, 7 October 2017
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	==~~HALOFERAX MEDITERRANEI GLUCOSE DEHYDROGENASE IN COMPLEX WITH~~ NADPH ~~AND ZN~~.==
			==Haloferax mediterranei glucose dehydrogenase in complex with NADPH and Zn.==
	<StructureSection load='2vwp' size='340' side='right' caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='2vwp' size='340' side='right' caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vwg\|2vwg]], [[2b5w\|2b5w]], [[2b5v\|2b5v]], [[2vwh\|2vwh]], [[2vwq\|2vwq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vwg\|2vwg]], [[2b5w\|2b5w]], [[2b5v\|2b5v]], [[2vwh\|2vwh]], [[2vwq\|2vwq]]</td></tr>
	<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>		<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>
	<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=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [http://pdbe.org/2vwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [http://www.ebi.ac.uk/pdbsum/2vwp 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=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [http://pdbe.org/2vwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [http://www.ebi.ac.uk/pdbsum/2vwp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2vwp ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 11:58, 9 February 2016

2016-02-09T11:58:31Z

← Older revision		Revision as of 11:58, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='2vwp' size='340' side='right' caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>		<StructureSection load='2vwp' size='340' side='right' caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vwp]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VWP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vwp]] 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=2VWP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VWP FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vwg\|2vwg]], [[2b5w\|2b5w]], [[2b5v\|2b5v]], [[2vwh\|2vwh]], [[2vwq\|2vwq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vwg\|2vwg]], [[2b5w\|2b5w]], [[2b5v\|2b5v]], [[2vwh\|2vwh]], [[2vwq\|2vwq]]</td></tr>
	<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>		<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>
	<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=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [http://www.ebi.ac.uk/pdbsum/2vwp 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=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [http://pdbe.org/2vwp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [http://www.ebi.ac.uk/pdbsum/2vwp PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/~~Q977U7_HALME Q977U7_HALME~~]] 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>		[[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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2vwp ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 28:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
			<div class="pdbe-citations 2vwp" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Atcc 33500]]
	[[Category: Glucose 1-dehydrogenase]]		[[Category: Glucose 1-dehydrogenase]]
	~~[[Category: Haloferax mediterranei]]~~
	[[Category: Baker, P J]]		[[Category: Baker, P J]]
	[[Category: Bonete, M J]]		[[Category: Bonete, M J]]

OCA at 06:40, 25 December 2014

2014-12-25T06:40:08Z

← Older revision		Revision as of 06:40, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2vwp]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VWP FirstGlance]. <br>		<table><tr><td colspan='2'>[[2vwp]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VWP FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vwg\|2vwg]], [[2b5w\|2b5w]], [[2b5v\|2b5v]], [[2vwh\|2vwh]], [[2vwq\|2vwq]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vwg\|2vwg]], [[2b5w\|2b5w]], [[2b5v\|2b5v]], [[2vwh\|2vwh]], [[2vwq\|2vwq]]</td></tr>
	<tr><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>		<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>
	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [http://www.ebi.ac.uk/pdbsum/2vwp 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=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [http://www.ebi.ac.uk/pdbsum/2vwp PDBsum]</span></td></tr>
	<table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/Q977U7_HALME Q977U7_HALME]] 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]]
Line 32:		Line 34:
	[[Category: Glucose 1-dehydrogenase]]		[[Category: Glucose 1-dehydrogenase]]
	[[Category: Haloferax mediterranei]]		[[Category: Haloferax mediterranei]]
	[[Category: Baker, P J.]]		[[Category: Baker, P J]]
	[[Category: Bonete, M J.]]		[[Category: Bonete, M J]]
	[[Category: Britton, K L.]]		[[Category: Britton, K L]]
	[[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, D W]]
	[[Category: Alcohol dehydrogenase]]		[[Category: Alcohol dehydrogenase]]
	[[Category: Glucose dehydrogenase]]		[[Category: Glucose dehydrogenase]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Zinc dependent medium chain alcohol dehydrogenase family]]		[[Category: Zinc dependent medium chain alcohol dehydrogenase family]]

OCA at 02:11, 1 October 2014

2014-10-01T02:11:19Z

← Older revision		Revision as of 02:11, 1 October 2014
Line 1:		Line 1:
	[[Image:~~2vwp~~.~~png~~\|~~left~~\|~~200px~~]]		==HALOFERAX MEDITERRANEI GLUCOSE DEHYDROGENASE IN COMPLEX WITH NADPH AND ZN.==
			<StructureSection load='2vwp' size='340' side='right' caption='[[2vwp]], [[Resolution\|resolution]] 2.01Å' scene=''>
			== Structural highlights ==
			<table><tr><td colspan='2'>[[2vwp]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2VWP FirstGlance]. <br>
			</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
			<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2vwg\|2vwg]], [[2b5w\|2b5w]], [[2b5v\|2b5v]], [[2vwh\|2vwh]], [[2vwq\|2vwq]]</td></tr>
			<tr><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>
			<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2vwp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vwp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2vwp RCSB], [http://www.ebi.ac.uk/pdbsum/2vwp PDBsum]</span></td></tr>
			<table>
			== Evolutionary Conservation ==
			[[Image:Consurf_key_small.gif\|200px\|right]]
			Check<jmol>
			<jmolCheckbox>
			<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vw/2vwp_consurf.spt"</scriptWhenChecked>
			<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
			<text>to colour the structure by Evolutionary Conservation</text>
			</jmolCheckbox>
			</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
			<div style="clear:both"></div>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			Despite being the subject of intensive investigations, many aspects of the mechanism of the zinc-dependent medium chain alcohol dehydrogenase (MDR) superfamily remain contentious. We have determined the high-resolution structures of a series of binary and ternary complexes of glucose dehydrogenase, an MDR enzyme from Haloferax mediterranei. In stark contrast to the textbook MDR mechanism in which the zinc ion is proposed to remain stationary and attached to a common set of protein ligands, analysis of these structures reveals that in each complex, there are dramatic differences in the nature of the zinc ligation. These changes arise as a direct consequence of linked movements of the zinc ion, a zinc-bound bound water molecule, and the substrate during progression through the reaction. These results provide evidence for the molecular basis of proton traffic during catalysis, a structural explanation for pentacoordinate zinc ion intermediates, a unifying view for the observed patterns of metal ligation in the MDR family, and highlight the importance of dynamic fluctuations at the metal center in changing the electrostatic potential in the active site, thereby influencing the proton traffic and hydride transfer events.

	~~{{STRUCTURE_2vwp\| PDB=2vwp \| SCENE= }}~~		Active site dynamics in the zinc-dependent medium chain alcohol dehydrogenase superfamily.,Baker PJ, Britton KL, Fisher M, Esclapez J, Pire C, Bonete MJ, Ferrer J, Rice DW Proc Natl Acad Sci U S A. 2009 Jan 8. PMID:19131516<ref>PMID:19131516</ref>

	~~===HALOFERAX MEDITERRANEI GLUCOSE DEHYDROGENASE IN COMPLEX WITH NADPH AND ZN.===~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
			</div>
	~~{{ABSTRACT_PUBMED_19131516}}~~		== References ==
			<references/>
	~~==About this Structure==~~		__TOC__
	~~[[2vwp]] is~~ a ~~1 chain structure with sequence from [http://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].~~		</StructureSection>

	==~~Reference~~==
	<~~ref group="xtra">PMID:019131516<~~/~~ref~~><~~references group="xtra"~~/>
	[[Category: Glucose 1-dehydrogenase]]		[[Category: Glucose 1-dehydrogenase]]
	[[Category: Haloferax mediterranei]]		[[Category: Haloferax mediterranei]]

OCA: Protected "2vwp" [edit=sysop:move=sysop]

2013-01-07T23:07:40Z

Protected "2vwp" [edit=sysop:move=sysop]

← Older revision	Revision as of 23:07, 7 January 2013
(No difference)

OCA at 23:07, 7 January 2013

2013-01-07T23:07:37Z

← Older revision		Revision as of 23:07, 7 January 2013
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	~~{{Seed}}~~
	[[Image:2vwp.png\|left\|200px]]		[[Image:2vwp.png\|left\|200px]]

	~~<!--~~
	~~The line below this paragraph, containing "STRUCTURE_2vwp", creates the "Structure Box" on the page.~~
	~~You may change the PDB parameter (which sets the PDB file loaded into the applet)~~
	~~or the SCENE parameter (which sets the initial scene displayed when the page is loaded),~~
	~~or leave the SCENE parameter empty for the default display.~~
	~~-->~~
	{{STRUCTURE_2vwp\| PDB=2vwp \| SCENE= }}		{{STRUCTURE_2vwp\| PDB=2vwp \| SCENE= }}

	===HALOFERAX MEDITERRANEI GLUCOSE DEHYDROGENASE IN COMPLEX WITH NADPH AND ZN.===		===HALOFERAX MEDITERRANEI GLUCOSE DEHYDROGENASE IN COMPLEX WITH NADPH AND ZN.===


	~~<!--~~
	~~The line below this paragraph, {{ABSTRACT_PUBMED_19131516}}, adds the Publication Abstract to the page~~
	~~(as it appears on PubMed at http://www.pubmed.gov), where 19131516 is the PubMed ID number.~~
	~~-->~~
	{{ABSTRACT_PUBMED_19131516}}		{{ABSTRACT_PUBMED_19131516}}

	==About this Structure==		==About this Structure==
	~~2VWP~~ is a 1 chain structure with sequence from [http://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].		[[2vwp]] is a 1 chain structure with sequence from [http://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].

	==Reference==		==Reference==
	<ref group="xtra">PMID:~~19131516~~</ref><references group="xtra"/>		<ref group="xtra">PMID:019131516</ref><references group="xtra"/>
	[[Category: Glucose 1-dehydrogenase]]		[[Category: Glucose 1-dehydrogenase]]
	[[Category: Haloferax mediterranei]]		[[Category: Haloferax mediterranei]]
Line 38:		Line 26:
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Zinc dependent medium chain alcohol dehydrogenase family]]		[[Category: Zinc dependent medium chain alcohol dehydrogenase family]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 11:55:18 2010''~~

OCA at 08:46, 22 September 2010

2010-09-22T08:46:19Z

← Older revision		Revision as of 08:46, 22 September 2010
Line 20:		Line 20:

	==About this Structure==		==About this Structure==
	2VWP is a ~~[[Single protein]]~~ structure of sequence from [http://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].		2VWP is a 1 chain structure with sequence from [http://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].

	==Reference==		==Reference==
	Active site dynamics in the zinc-dependent medium chain alcohol dehydrogenase superfamily., Baker PJ, Britton KL, Fisher M, Esclapez J, Pire C, Bonete MJ, Ferrer J, Rice DW, Proc Natl Acad Sci U S A. 2009 Jan 8. PMID:~~[http://www.ncbi.nlm.nih.gov~~/~~pubmed~~/~~19131516 19131516]~~		<ref group="xtra">PMID:19131516</ref><references group="xtra"/>
	[[Category: Glucose 1-dehydrogenase]]		[[Category: Glucose 1-dehydrogenase]]
	[[Category: Haloferax mediterranei]]		[[Category: Haloferax mediterranei]]
	[[Category: ~~Single protein~~]]		[[Category: Baker, P J.]]
	[[Category: ~~Pdbx_ordinal=~~, ~~<PDBx~~:~~audit_author~~.]]		[[Category: Bonete, M J.]]
			[[Category: Britton, K L.]]
			[[Category: Esclapez, J.]]
			[[Category: Ferrer, J.]]
			[[Category: Fisher, M.]]
			[[Category: Pire, C.]]
			[[Category: Rice, D W.]]
	[[Category: Alcohol dehydrogenase]]		[[Category: Alcohol dehydrogenase]]
	[[Category: Glucose dehydrogenase]]		[[Category: Glucose dehydrogenase]]
Line 33:		Line 39:
	[[Category: Zinc dependent medium chain alcohol dehydrogenase family]]		[[Category: Zinc dependent medium chain alcohol dehydrogenase family]]

	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Feb 4 20~~:12:~~43 2009~~''		''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 11:55:18 2010''