2zj3 - Revision history

OCA at 13:37, 1 November 2023

OCA — Wed, 01 Nov 2023 13:37:03 GMT

←Older revision		Revision as of 13:37, 1 November 2023
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	<StructureSection load='2zj3' size='340' side='right'caption='[[2zj3]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2zj3' size='340' side='right'caption='[[2zj3]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zj3]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=2ZJ3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zj3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZJ3 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=G6P:ALPHA~~-~~D-GLUCOSE-6-PHOSPHATE'>G6P</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]] 1.9Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~>[[2zj4\|2zj4]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks'>[http~~:~~//en.wikipedia.org/wiki/Glutamine~~--~~fructose~~-6-~~phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16]~~ </~~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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [https://pdbe.org/2zj3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [https://www.ebi.ac.uk/pdbsum/2zj3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zj3 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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [~~http~~://pdbe.org/2zj3 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2zj3 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2zj3 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Defects in GFPT1 are the cause of myasthenia, congenital, with tubular aggregates, type 1 (CMSTA1) [MIM:[~~http~~://omim.org/entry/610542 610542]]. A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.<ref>PMID:21310273</ref>	+	[https://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN] Defects in GFPT1 are the cause of myasthenia, congenital, with tubular aggregates, type 1 (CMSTA1) [MIM:[https://omim.org/entry/610542 610542]. A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.<ref>PMID:21310273</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.	+	[https://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN] Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
	== 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: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bando, M]]	+	[[Category: Bando M]]
-	[[Category: Kondo, K]]	+	[[Category: Kondo K]]
-	[[Category: Nakaishi, Y]]	+	[[Category: Nakaishi Y]]
-	[[Category: Tsuge, H]]	+	[[Category: Tsuge H]]
-	~~[[Category: Aldose/ketose isomerase]]~~	+
-	~~[[Category: Alternative splicing]]~~	+
-	~~[[Category: Aminotransferase]]~~	+
-	~~[[Category: Glucosamine-6-phosphate synthase]]~~	+
-	~~[[Category: Glutamine amidotransferase]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: Rossmann-like fold]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 12:05, 29 July 2020

OCA — Wed, 29 Jul 2020 12:05:29 GMT

←Older revision		Revision as of 12:05, 29 July 2020
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	==Isomerase domain of human glucose:fructose-6-phosphate amidotransferase==		==Isomerase domain of human glucose:fructose-6-phosphate amidotransferase==
-	<StructureSection load='2zj3' size='340' side='right' caption='[[2zj3]], [[Resolution\|resolution]] 1.90Å' scene=''>	+	<StructureSection load='2zj3' size='340' side='right'caption='[[2zj3]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2ZJ3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2ZJ3 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zj4\|2zj4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zj4\|2zj4]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [http://pdbe.org/2zj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zj3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zj3 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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [http://pdbe.org/2zj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zj3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zj3 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 37:		Line 37:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Bando, M]]		[[Category: Bando, M]]
	[[Category: Kondo, K]]		[[Category: Kondo, K]]

OCA at 07:06, 18 October 2018

OCA — Thu, 18 Oct 2018 07:06:31 GMT

←Older revision		Revision as of 07:06, 18 October 2018
Line 1:		Line 1:
		+
	==Isomerase domain of human glucose:fructose-6-phosphate amidotransferase==		==Isomerase domain of human glucose:fructose-6-phosphate amidotransferase==
	<StructureSection load='2zj3' size='340' side='right' caption='[[2zj3]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2zj3' size='340' side='right' caption='[[2zj3]], [[Resolution\|resolution]] 1.90Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zj4\|2zj4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zj4\|2zj4]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [http://pdbe.org/2zj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zj3 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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [http://pdbe.org/2zj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zj3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2zj3 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 16:		Line 17:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zj/2zj3_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zj/2zj3_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: Tsuge, H]]		[[Category: Tsuge, H]]
	[[Category: Aldose/ketose isomerase]]		[[Category: Aldose/ketose isomerase]]
		+	[[Category: Alternative splicing]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]
	[[Category: Glucosamine-6-phosphate synthase]]		[[Category: Glucosamine-6-phosphate synthase]]

OCA at 11:05, 9 February 2016

OCA — Tue, 09 Feb 2016 11:05:50 GMT

←Older revision		Revision as of 11:05, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='2zj3' size='340' side='right' caption='[[2zj3]], [[Resolution\|resolution]] 1.90Å' scene=''>		<StructureSection load='2zj3' size='340' side='right' caption='[[2zj3]], [[Resolution\|resolution]] 1.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZJ3 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZJ3 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zj4\|2zj4]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zj4\|2zj4]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zj3 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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [http://pdbe.org/2zj3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zj3 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 20:
	<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=2zj3 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
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	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 2zj3" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Bando, M]]		[[Category: Bando, M]]
	[[Category: Kondo, K]]		[[Category: Kondo, K]]

OCA at 11:20, 20 January 2015

OCA — Tue, 20 Jan 2015 11:20:34 GMT

←Older revision		Revision as of 11:20, 20 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZJ3 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZJ3 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zj4\|2zj4]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zj4\|2zj4]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zj3 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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zj3 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Defects in GFPT1 are the cause of myasthenia, congenital, with tubular aggregates, type 1 (CMSTA1) [MIM:[http://omim.org/entry/610542 610542]]. A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.<ref>PMID:21310273</ref>		[[http://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Defects in GFPT1 are the cause of myasthenia, congenital, with tubular aggregates, type 1 (CMSTA1) [MIM:[http://omim.org/entry/610542 610542]]. A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.<ref>PMID:21310273</ref>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Bando, M.]]	+	[[Category: Bando, M]]
-	[[Category: Kondo, K.]]	+	[[Category: Kondo, K]]
-	[[Category: Nakaishi, Y.]]	+	[[Category: Nakaishi, Y]]
-	[[Category: Tsuge, H.]]	+	[[Category: Tsuge, H]]
	[[Category: Aldose/ketose isomerase]]		[[Category: Aldose/ketose isomerase]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]

OCA at 05:24, 2 October 2014

OCA — Thu, 02 Oct 2014 05:24:43 GMT

←Older revision		Revision as of 05:24, 2 October 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2zj3\| PDB=2zj3 \| SCENE= }}~~	+	==Isomerase domain of human glucose:fructose-6-phosphate amidotransferase==
-	===Isomerase domain of human glucose:fructose-6-phosphate amidotransferase===	+	<StructureSection load='2zj3' size='340' side='right' caption='[[2zj3]], [[Resolution\|resolution]] 1.90Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19059404}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZJ3 FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=G6P:ALPHA-D-GLUCOSE-6-PHOSPHATE'>G6P</scene><br>
-	[[http://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Defects in GFPT1 are the cause of myasthenia, congenital, with tubular aggregates, type 1 (CMSTA1) [MIM:[http://omim.org/entry/610542 610542]]. A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.<ref>PMID:21310273</ref>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2zj4\|2zj4]]</td></tr>
-		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamine--fructose-6-phosphate_transaminase_(isomerizing) Glutamine--fructose-6-phosphate transaminase (isomerizing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.16 2.6.1.16] </span></td></tr>
-	==Function==	+	<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=2zj3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zj3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zj3 RCSB], [http://www.ebi.ac.uk/pdbsum/2zj3 PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Defects in GFPT1 are the cause of myasthenia, congenital, with tubular aggregates, type 1 (CMSTA1) [MIM:[http://omim.org/entry/610542 610542]]. A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.<ref>PMID:21310273</ref>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.		[[http://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
		+	== 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/zj/2zj3_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 ==
		+	Glutamine:fructose-6-phosphate amidotransferase (GFAT) is a rate-limiting enzyme in the hexoamine biosynthetic pathway and plays an important role in type 2 diabetes. We now report the first structures of the isomerase domain of the human GFAT in the presence of cyclic glucose-6-phosphate and linear glucosamine-6-phosphate. The C-terminal tail including the active site displays a rigid conformation, similar to the corresponding Escherichia coli enzyme. The diversity of the CF helix near the active site suggests the helix is a major target for drug design. Our study provides insights into the development of therapeutic drugs for type 2 diabetes.

-	~~==About this Structure==~~	+	Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes.,Nakaishi Y, Bando M, Shimizu H, Watanabe K, Goto F, Tsuge H, Kondo K, Komatsu M FEBS Lett. 2009 Jan 5;583(1):163-7. Epub 2008 Dec 6. PMID:19059404<ref>PMID:19059404</ref>
-	~~[[2zj3]] is~~ a 1 ~~chain structure with sequence from [http~~:~~//en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http~~:/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bando, M.]]		[[Category: Bando, M.]]

OCA at 06:41, 25 March 2013

OCA — Mon, 25 Mar 2013 06:41:29 GMT

←Older revision		Revision as of 06:41, 25 March 2013
Line 1:		Line 1:
-	[[Image:2zj3.png\|left\|200px]]
-
	{{STRUCTURE_2zj3\| PDB=2zj3 \| SCENE= }}		{{STRUCTURE_2zj3\| PDB=2zj3 \| SCENE= }}
-
	===Isomerase domain of human glucose:fructose-6-phosphate amidotransferase===		===Isomerase domain of human glucose:fructose-6-phosphate amidotransferase===
-
	{{ABSTRACT_PUBMED_19059404}}		{{ABSTRACT_PUBMED_19059404}}
		+
		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Defects in GFPT1 are the cause of myasthenia, congenital, with tubular aggregates, type 1 (CMSTA1) [MIM:[http://omim.org/entry/610542 610542]]. A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors.<ref>PMID:21310273</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/GFPT1_HUMAN GFPT1_HUMAN]] Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.

	==About this Structure==		==About this Structure==
	[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA].		[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bando, M.]]		[[Category: Bando, M.]]

OCA: Protected "2zj3" [edit=sysop:move=sysop]

OCA — Mon, 07 Jan 2013 22:53:33 GMT

Protected "2zj3" [edit=sysop:move=sysop]

←Older revision

Revision as of 22:53, 7 January 2013

OCA at 22:53, 7 January 2013

OCA — Mon, 07 Jan 2013 22:53:28 GMT

←Older revision		Revision as of 22:53, 7 January 2013
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:2zj3.png\|left\|200px]]
-	[[Image:2zj3.~~jpg~~\|left\|200px]]	+

-	<!--
-	The line below this paragraph, containing "STRUCTURE_2zj3", 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_2zj3\| PDB=2zj3 \| SCENE= }}		{{STRUCTURE_2zj3\| PDB=2zj3 \| SCENE= }}

	===Isomerase domain of human glucose:fructose-6-phosphate amidotransferase===		===Isomerase domain of human glucose:fructose-6-phosphate amidotransferase===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19059404}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19059404 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19059404}}		{{ABSTRACT_PUBMED_19059404}}

	==About this Structure==		==About this Structure==
-	~~2ZJ3~~ is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA].	+	[[2zj3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA].
-		+
-	~~==Reference==~~	+
-	Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes., Nakaishi Y, Bando M, Shimizu H, Watanabe K, Goto F, Tsuge H, Kondo K, Komatsu M, FEBS Lett. 2009 Jan 5;583(1):163-7. Epub 2008 Dec 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19059404 19059404]	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Bando, M.]]		[[Category: Bando, M.]]
Line 30:		Line 15:
	[[Category: Tsuge, H.]]		[[Category: Tsuge, H.]]
	[[Category: Aldose/ketose isomerase]]		[[Category: Aldose/ketose isomerase]]
-	[[Category: Alternative splicing]]
	[[Category: Aminotransferase]]		[[Category: Aminotransferase]]
-	[[Category: Crystal structure]]
	[[Category: Glucosamine-6-phosphate synthase]]		[[Category: Glucosamine-6-phosphate synthase]]
	[[Category: Glutamine amidotransferase]]		[[Category: Glutamine amidotransferase]]
Line 38:		Line 21:
	[[Category: Rossmann-like fold]]		[[Category: Rossmann-like fold]]
	[[Category: Transferase]]		[[Category: Transferase]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 14 13:10:59 2009''

OCA at 11:10, 14 January 2009

OCA — Wed, 14 Jan 2009 11:10:59 GMT

←Older revision		Revision as of 11:10, 14 January 2009
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:2zj3.jpg\|left\|200px]]

-	The ~~entry 2zj3~~ is ~~ON HOLD~~ ~~until Mar 01 2010~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_2zj3", 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_2zj3\| PDB=2zj3 \| SCENE= }}

-	~~Authors~~: ~~Nakaishi, Y.~~	+	===Isomerase domain of human glucose:fructose-6-phosphate amidotransferase===

-	Description: Isomerase domain of human glucose:fructose-6-phosphate amidotransferase

		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_19059404}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 19059404 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_19059404}}

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Jun 11 09~~:10:~~15 2008~~''	+	==About this Structure==
		+	2ZJ3 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZJ3 OCA].
		+
		+	==Reference==
		+	Structural analysis of human glutamine:fructose-6-phosphate amidotransferase, a key regulator in type 2 diabetes., Nakaishi Y, Bando M, Shimizu H, Watanabe K, Goto F, Tsuge H, Kondo K, Komatsu M, FEBS Lett. 2009 Jan 5;583(1):163-7. Epub 2008 Dec 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/19059404 19059404]
		+	[[Category: Homo sapiens]]
		+	[[Category: Bando, M.]]
		+	[[Category: Kondo, K.]]
		+	[[Category: Nakaishi, Y.]]
		+	[[Category: Tsuge, H.]]
		+	[[Category: Aldose/ketose isomerase]]
		+	[[Category: Alternative splicing]]
		+	[[Category: Aminotransferase]]
		+	[[Category: Crystal structure]]
		+	[[Category: Glucosamine-6-phosphate synthase]]
		+	[[Category: Glutamine amidotransferase]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: Rossmann-like fold]]
		+	[[Category: Transferase]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 14 13:10:59 2009''