2wfa - Revision history

OCA at 17:35, 8 September 2026

2026-09-08T17:35:50Z

← Older revision		Revision as of 17:35, 8 September 2026
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	<jmolCheckbox>		<jmolCheckbox>
	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wf/2wfa_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wf/2wfa_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/~~initialview01~~.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>

OCA at 10:12, 9 May 2024

2024-05-09T10:12:02Z

← Older revision		Revision as of 10:12, 9 May 2024
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	<StructureSection load='2wfa' size='340' side='right'caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='2wfa' size='340' side='right'caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~"bacterium_lactis"_lister_1873 "bacterium~~ lactis~~" lister 1873~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WFA FirstGlance]. <br>		<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WFA FirstGlance]. <br>
	</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=MG:MAGNESIUM+ION'>MG</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]] 1.65Å</td></tr>
	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1z4o\|1z4o]], [[2wf5\|2wf5]], [[1o03\|1o03]], [[1zol\|1zol]], [[1z4n\|1z4n]], [[1lvh\|1lvh]], [[1o08\|1o08]], [[2wf6\|2wf6]], [[2wf8\|2wf8]], [[2wf7\|2wf7]], [[2wf9\|2wf9]]~~</~~div~~><~~/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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b></td><td class="sblockDat"><span class='plainlinks~~'>~~[https://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [https://pdbe.org/2wfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [https://www.ebi.ac.uk/pdbsum/2wfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfa 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=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [https://pdbe.org/2wfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [https://www.ebi.ac.uk/pdbsum/2wfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://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>		[https://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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 37:		Line 36:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Bacterium~~ lactis ~~lister 1873]]~~		[[Category: Lactococcus lactis]]
	~~[[Category: Beta-phosphoglucomutase~~]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Alizadeh, T]]		[[Category: Alizadeh T]]
	[[Category: Baxter~~, N J~~]]		[[Category: Baxter NJ]]
	[[Category: Bermel, W]]		[[Category: Bermel W]]
	[[Category: Blackburn~~, G M~~]]		[[Category: Blackburn GM]]
	[[Category: Bowler~~, M W~~]]		[[Category: Bowler MW]]
	[[Category: Cliff~~, M J~~]]		[[Category: Cliff MJ]]
	[[Category: Hollfelder, F]]		[[Category: Hollfelder F]]
	[[Category: Hounslow~~, A M~~]]		[[Category: Hounslow AM]]
	[[Category: Pollard, S]]		[[Category: Pollard S]]
	[[Category: Waltho~~, J P~~]]		[[Category: Waltho JP]]
	[[Category: Webster~~, C E~~]]		[[Category: Webster CE]]
	[[Category: Williams~~, N H]]~~		[[Category: Williams NH]]
	~~[[Category: Haloacid dehalogenase superfamily]]~~
	~~[[Category: Isomerase]]~~
	~~[[Category: Phosphotransferase]]~~
	~~[[Category: Transition state analogue~~]]

OCA at 11:05, 6 April 2022

2022-04-06T11:05:51Z

← Older revision		Revision as of 11:05, 6 April 2022
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	<StructureSection load='2wfa' size='340' side='right'caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='2wfa' size='340' side='right'caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2WFA FirstGlance]. <br>		<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WFA FirstGlance]. <br>
	</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=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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z4o\|1z4o]], [[2wf5\|2wf5]], [[1o03\|1o03]], [[1zol\|1zol]], [[1z4n\|1z4n]], [[1lvh\|1lvh]], [[1o08\|1o08]], [[2wf6\|2wf6]], [[2wf8\|2wf8]], [[2wf7\|2wf7]], [[2wf9\|2wf9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1z4o\|1z4o]], [[2wf5\|2wf5]], [[1o03\|1o03]], [[1zol\|1zol]], [[1z4n\|1z4n]], [[1lvh\|1lvh]], [[1o08\|1o08]], [[2wf6\|2wf6]], [[2wf8\|2wf8]], [[2wf7\|2wf7]], [[2wf9\|2wf9]]</div></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'>[https://en.wikipedia.org/wiki/Beta-phosphoglucomutase Beta-phosphoglucomutase], with EC number [https://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~~://proteopedia.org/fgij/fg.htm?mol=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [~~http~~://pdbe.org/2wfa PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2wfa PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfa 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=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [https://pdbe.org/2wfa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [https://www.ebi.ac.uk/pdbsum/2wfa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfa 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>		[[https://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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:39, 1 July 2020

2020-07-01T08:39:04Z

← Older revision		Revision as of 08:39, 1 July 2020
Line 1:		Line 1:

	==Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.==		==Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.==
	<StructureSection load='2wfa' size='340' side='right' caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='2wfa' size='340' side='right'caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2WFA FirstGlance]. <br>		<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2WFA 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=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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z4o\|1z4o]], [[2wf5\|2wf5]], [[1o03\|1o03]], [[1zol\|1zol]], [[1z4n\|1z4n]], [[1lvh\|1lvh]], [[1o08\|1o08]], [[2wf6\|2wf6]], [[2wf8\|2wf8]], [[2wf7\|2wf7]], [[2wf9\|2wf9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z4o\|1z4o]], [[2wf5\|2wf5]], [[1o03\|1o03]], [[1zol\|1zol]], [[1z4n\|1z4n]], [[1lvh\|1lvh]], [[1o08\|1o08]], [[2wf6\|2wf6]], [[2wf8\|2wf8]], [[2wf7\|2wf7]], [[2wf9\|2wf9]]</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://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [http://pdbe.org/2wfa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [http://www.ebi.ac.uk/pdbsum/2wfa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfa ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [http://pdbe.org/2wfa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [http://www.ebi.ac.uk/pdbsum/2wfa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 32:		Line 32:

	==See Also==		==See Also==
	*[[Beta-phosphoglucomutase\|Beta-phosphoglucomutase]]		*[[Beta-phosphoglucomutase 3D structures\|Beta-phosphoglucomutase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 39:		Line 39:
	[[Category: Bacterium lactis lister 1873]]		[[Category: Bacterium lactis lister 1873]]
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
			[[Category: Large Structures]]
	[[Category: Alizadeh, T]]		[[Category: Alizadeh, T]]
	[[Category: Baxter, N J]]		[[Category: Baxter, N J]]

OCA at 09:48, 26 September 2018

2018-09-26T09:48:42Z

← Older revision		Revision as of 09:48, 26 September 2018
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/wf/2wfa_consurf.spt"</scriptWhenChecked>		<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wf/2wfa_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>

OCA at 11:43, 5 August 2016

2016-08-05T11:43:04Z

← Older revision		Revision as of 11:43, 5 August 2016
Line 1:		Line 1:

	==Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.==		==Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.==
	<StructureSection load='2wfa' size='340' side='right' caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='2wfa' size='340' side='right' caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Lactococcus_lactis Lactococcus~~ lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WFA FirstGlance]. <br>		<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WFA 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=MG:MAGNESIUM+ION'>MG</scene></td></tr>		</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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z4o\|1z4o]], [[2wf5\|2wf5]], [[1o03\|1o03]], [[1zol\|1zol]], [[1z4n\|1z4n]], [[1lvh\|1lvh]], [[1o08\|1o08]], [[2wf6\|2wf6]], [[2wf8\|2wf8]], [[2wf7\|2wf7]], [[2wf9\|2wf9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z4o\|1z4o]], [[2wf5\|2wf5]], [[1o03\|1o03]], [[1zol\|1zol]], [[1z4n\|1z4n]], [[1lvh\|1lvh]], [[1o08\|1o08]], [[2wf6\|2wf6]], [[2wf8\|2wf8]], [[2wf7\|2wf7]], [[2wf9\|2wf9]]</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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [http://www.ebi.ac.uk/pdbsum/2wfa 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=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [http://pdbe.org/2wfa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [http://www.ebi.ac.uk/pdbsum/2wfa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2wfa ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<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=2wfa ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	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 2wfa" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 35:		Line 37:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
			[[Category: Bacterium lactis lister 1873]]
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
	~~[[Category: Lactococcus lactis]]~~
	[[Category: Alizadeh, T]]		[[Category: Alizadeh, T]]
	[[Category: Baxter, N J]]		[[Category: Baxter, N J]]

OCA at 02:07, 25 December 2014

2014-12-25T02:07:57Z

← Older revision		Revision as of 02:07, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='2wfa' size='340' side='right' caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>		<StructureSection load='2wfa' size='340' side='right' caption='[[2wfa]], [[Resolution\|resolution]] 1.65Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. <br>		<table><tr><td colspan='2'>[[2wfa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2WFA FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z4o\|1z4o]], [[2wf5\|2wf5]], [[1o03\|1o03]], [[1zol\|1zol]], [[1z4n\|1z4n]], [[1lvh\|1lvh]], [[1o08\|1o08]], [[2wf6\|2wf6]], [[2wf8\|2wf8]], [[2wf7\|2wf7]], [[2wf9\|2wf9]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1z4o\|1z4o]], [[2wf5\|2wf5]], [[1o03\|1o03]], [[1zol\|1zol]], [[1z4n\|1z4n]], [[1lvh\|1lvh]], [[1o08\|1o08]], [[2wf6\|2wf6]], [[2wf8\|2wf8]], [[2wf7\|2wf7]], [[2wf9\|2wf9]]</td></tr>
	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.~~7.1~~.2 2.7.1.2] </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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [http://www.ebi.ac.uk/pdbsum/2wfa 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=2wfa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wfa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2wfa RCSB], [http://www.ebi.ac.uk/pdbsum/2wfa PDBsum]</span></td></tr>
	<table>		</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>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 24:		Line 26:
	Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.,Griffin JL, Bowler MW, Baxter NJ, Leigh KN, Dannatt HR, Hounslow AM, Blackburn GM, Webster CE, Cliff MJ, Waltho JP Proc Natl Acad Sci U S A. 2012 May 1;109(18):6910-5. Epub 2012 Apr 13. PMID:22505741<ref>PMID:22505741</ref>		Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.,Griffin JL, Bowler MW, Baxter NJ, Leigh KN, Dannatt HR, Hounslow AM, Blackburn GM, Webster CE, Cliff MJ, Waltho JP Proc Natl Acad Sci U S A. 2012 May 1;109(18):6910-5. Epub 2012 Apr 13. PMID:22505741<ref>PMID:22505741</ref>

	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>

			==See Also==
			*[[Beta-phosphoglucomutase\|Beta-phosphoglucomutase]]
	== References ==		== References ==
	<references/>		<references/>
Line 32:		Line 37:
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
	[[Category: Lactococcus lactis]]		[[Category: Lactococcus lactis]]
	[[Category: Alizadeh, T.]]		[[Category: Alizadeh, T]]
	[[Category: Baxter, N J.]]		[[Category: Baxter, N J]]
	[[Category: Bermel, W.]]		[[Category: Bermel, W]]
	[[Category: Blackburn, G M.]]		[[Category: Blackburn, G M]]
	[[Category: Bowler, M W.]]		[[Category: Bowler, M W]]
	[[Category: Cliff, M J.]]		[[Category: Cliff, M J]]
	[[Category: Hollfelder, F.]]		[[Category: Hollfelder, F]]
	[[Category: Hounslow, A M.]]		[[Category: Hounslow, A M]]
	[[Category: Pollard, S.]]		[[Category: Pollard, S]]
	[[Category: Waltho, J P.]]		[[Category: Waltho, J P]]
	[[Category: Webster, C E.]]		[[Category: Webster, C E]]
	[[Category: Williams, N H.]]		[[Category: Williams, N H]]
	[[Category: Haloacid dehalogenase superfamily]]		[[Category: Haloacid dehalogenase superfamily]]
	[[Category: Isomerase]]		[[Category: Isomerase]]
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]
	[[Category: Transition state analogue]]		[[Category: Transition state analogue]]

OCA at 08:43, 7 May 2014

2014-05-07T08:43:47Z

@@ Line 1: / Line 1: @@
-[[Image:2wfa.png|left|200px]]
+==Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.==
-<!--
+Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.,Griffin JL, Bowler MW, Baxter NJ, Leigh KN, Dannatt HR, Hounslow AM, Blackburn GM, Webster CE, Cliff MJ, Waltho JP Proc Natl Acad Sci U S A. 2012 May 1;109(18):6910-5. Epub 2012 Apr 13. PMID:22505741<ref>PMID:22505741</ref>
-===Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.===
+From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+</div>
+== References ==
-<!--
+<references/>
-The line below this paragraph, {{ABSTRACT_PUBMED_22505741}}, adds the Publication Abstract to the page
+__TOC__
-(as it appears on PubMed at http://www.pubmed.gov), where 22505741 is the PubMed ID number.
+</StructureSection>
 [[Category: Beta-phosphoglucomutase]]
 [[Category: Lactococcus lactis]]

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

2012-05-16T08:27:35Z

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

← Older revision	Revision as of 08:27, 16 May 2012
(No difference)

OCA at 08:27, 16 May 2012

2012-05-16T08:27:33Z

← Older revision		Revision as of 08:27, 16 May 2012
Line 1:		Line 1:
	~~{{Seed}}~~		[[Image:2wfa.png\|left\|200px]]
	[[Image:2wfa.~~jpg~~\|left\|200px]]

	<!--		<!--
Line 10:		Line 9:
	{{STRUCTURE_2wfa\| PDB=2wfa \| SCENE= }}		{{STRUCTURE_2wfa\| PDB=2wfa \| SCENE= }}

	===~~STRUCTURE OF BETA~~-~~PHOSPHOGLUCOMUTASE INHIBITED WITH BERYLLIUM TRIFLUORIDE~~, ~~IN AN OPEN CONFORMATION~~.===		===Structure of Beta-Phosphoglucomutase inhibited with Beryllium trifluoride, in an open conformation.===


			<!--
			The line below this paragraph, {{ABSTRACT_PUBMED_22505741}}, adds the Publication Abstract to the page
			(as it appears on PubMed at http://www.pubmed.gov), where 22505741 is the PubMed ID number.
			-->
			{{ABSTRACT_PUBMED_22505741}}

	==About this Structure==		==About this Structure==
	~~2WFA~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA].		[[2wfa]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WFA OCA].

			==Reference==
			<ref group="xtra">PMID:022505741</ref><references group="xtra"/>
	[[Category: Beta-phosphoglucomutase]]		[[Category: Beta-phosphoglucomutase]]
	[[Category: Lactococcus lactis]]		[[Category: Lactococcus lactis]]
Line 33:		Line 41:
	[[Category: Phosphotransferase]]		[[Category: Phosphotransferase]]
	[[Category: Transition state analogue]]		[[Category: Transition state analogue]]

	~~''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 26 08:28:06 2010''~~