2bh9 - Revision history

OCA at 06:38, 1 May 2024

OCA — Wed, 01 May 2024 06:38:01 GMT

←Older revision		Revision as of 06:38, 1 May 2024
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	<StructureSection load='2bh9' size='340' side='right'caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2bh9' size='340' side='right'caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2bh9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2bh9]] 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=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>~~, ~~<scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 2.5Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1qki\|1qki]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49]~~ </~~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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [https://pdbe.org/2bh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [https://www.ebi.ac.uk/pdbsum/2bh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bh9 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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [https://pdbe.org/2bh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [https://www.ebi.ac.uk/pdbsum/2bh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bh9 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[https://omim.org/entry/305900 305900]]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>	+	[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[https://omim.org/entry/305900 305900]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.	+	[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN] Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</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=2bh9 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=2bh9 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Human glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt. Binary complexes of the human deletion mutant, DeltaG6PD, with glucose-6-phosphate and NADP(+) have been crystallized and their structures solved to 2.9 and 2.5 A, respectively. The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site. Substrate binding in DeltaG6PD is shown to be very similar to that described previously in Leuconostoc mesenteroides G6PD. NADP(+) binding at the coenzyme site is seen to be comparable to NADP(+) binding in L. mesenteroides G6PD, although some differences arise as a result of sequence changes. The tetramer interface varies slightly among the human G6PD complexes, suggesting flexibility in the predominantly hydrophilic dimer-dimer interactions. In both complexes, Pro172 of the conserved peptide EKPxG is in the cis conformation; it is seen to be crucial for close approach of the substrate and coenzyme during the enzymatic reaction. Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered. The implications of possible interaction between the structural NADP(+) and G6P are considered.
-
-	Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase.,Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):495-504. Epub 2005, Apr 20. PMID:15858258<ref>PMID:15858258</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2bh9" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Glucose-6-phosphate dehydrogenase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Adams~~, M J~~]]	+	[[Category: Adams MJ]]
-	[[Category: Au~~, S W.N~~]]	+	[[Category: Au SWN]]
-	[[Category: Gover, S]]	+	[[Category: Gover S]]
-	[[Category: Vandeputte-Rutten, L]]	+	[[Category: Vandeputte-Rutten L]]
-	~~[[Category: Carbohydrate metabolism]]~~	+
-	~~[[Category: Glucose metabolism]]~~	+
-	~~[[Category: Oxidoreductase~~]]	+

OCA at 10:31, 17 February 2021

OCA — Wed, 17 Feb 2021 10:31:36 GMT

OCA at 11:50, 10 May 2019

OCA — Fri, 10 May 2019 11:50:40 GMT

←Older revision		Revision as of 11:50, 10 May 2019
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	==X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP==		==X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP==
-	<StructureSection load='2bh9' size='340' side='right' caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>	+	<StructureSection load='2bh9' size='340' side='right'caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bh9]] 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=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bh9]] 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=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>
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	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Adams, M J]]		[[Category: Adams, M J]]
	[[Category: Au, S W.N]]		[[Category: Au, S W.N]]

OCA at 06:11, 16 May 2018

OCA — Wed, 16 May 2018 06:11:33 GMT

←Older revision		Revision as of 06:11, 16 May 2018
Line 1:		Line 1:
		+
	==X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP==		==X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP==
	<StructureSection load='2bh9' size='340' side='right' caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2bh9' size='340' side='right' caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>
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	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [http://pdbe.org/2bh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/2bh9 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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [http://pdbe.org/2bh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/2bh9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2bh9 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/2bh9_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/2bh9_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>
	</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=2bh9 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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	</div>		</div>
	<div class="pdbe-citations 2bh9" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2bh9" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glucose 6-phosphate dehydrogenase\|Glucose 6-phosphate dehydrogenase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 11:09, 11 September 2015

OCA — Fri, 11 Sep 2015 11:09:28 GMT

←Older revision		Revision as of 11:09, 11 September 2015
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	<StructureSection load='2bh9' size='340' side='right' caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2bh9' size='340' side='right' caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2bh9]] 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=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2bh9]] 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=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/2bh9 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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [http://pdbe.org/2bh9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/2bh9 PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
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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 2bh9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
Line 35:		Line 36:
	</StructureSection>		</StructureSection>
	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Adams, M J]]		[[Category: Adams, M J]]
	[[Category: Au, S W.N]]		[[Category: Au, S W.N]]

OCA at 09:55, 8 January 2015

OCA — Thu, 08 Jan 2015 09:55:47 GMT

←Older revision		Revision as of 09:55, 8 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2bh9]] 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=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[2bh9]] 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=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/2bh9 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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/2bh9 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[http://omim.org/entry/305900 305900]]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>		[[http://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[http://omim.org/entry/305900 305900]]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>
Line 36:		Line 36:
	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Adams, M J.]]	+	[[Category: Adams, M J]]
-	[[Category: Au, S W.N.]]	+	[[Category: Au, S W.N]]
-	[[Category: Gover, S.]]	+	[[Category: Gover, S]]
-	[[Category: Vandeputte-Rutten, L.]]	+	[[Category: Vandeputte-Rutten, L]]
	[[Category: Carbohydrate metabolism]]		[[Category: Carbohydrate metabolism]]
	[[Category: Glucose metabolism]]		[[Category: Glucose metabolism]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 00:40, 30 September 2014

OCA — Tue, 30 Sep 2014 00:40:56 GMT

←Older revision		Revision as of 00:40, 30 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_2bh9\| PDB=2bh9 \| SCENE= }}~~	+	==X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP==
-	===X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP===	+	<StructureSection load='2bh9' size='340' side='right' caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_15858258}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[2bh9]] 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=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene><br>
-	[[http://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[http://omim.org/entry/305900 305900]]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>	+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]]</td></tr>
-		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucose-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [http://www.ebi.ac.uk/pdbsum/2bh9 PDBsum]</span></td></tr>
		+	<table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[http://omim.org/entry/305900 305900]]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.		[[http://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.
		+	== 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/bh/2bh9_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 ==
		+	Human glucose-6-phosphate dehydrogenase (G6PD) is NADP(+)-dependent and catalyses the first and rate-limiting step of the pentose phosphate shunt. Binary complexes of the human deletion mutant, DeltaG6PD, with glucose-6-phosphate and NADP(+) have been crystallized and their structures solved to 2.9 and 2.5 A, respectively. The structures are compared with the previously determined structure of the Canton variant of human G6PD (G6PD(Canton)) in which NADP(+) is bound at the structural site. Substrate binding in DeltaG6PD is shown to be very similar to that described previously in Leuconostoc mesenteroides G6PD. NADP(+) binding at the coenzyme site is seen to be comparable to NADP(+) binding in L. mesenteroides G6PD, although some differences arise as a result of sequence changes. The tetramer interface varies slightly among the human G6PD complexes, suggesting flexibility in the predominantly hydrophilic dimer-dimer interactions. In both complexes, Pro172 of the conserved peptide EKPxG is in the cis conformation; it is seen to be crucial for close approach of the substrate and coenzyme during the enzymatic reaction. Structural NADP(+) binds in a very similar way in the DeltaG6PD-NADP(+) complex and in G6PD(Canton), while in the substrate complex the structural NADP(+) has low occupancy and the C-terminal tail at the structural NADP(+) site is disordered. The implications of possible interaction between the structural NADP(+) and G6P are considered.

-	~~==About this Structure==~~	+	Structural studies of glucose-6-phosphate and NADP+ binding to human glucose-6-phosphate dehydrogenase.,Kotaka M, Gover S, Vandeputte-Rutten L, Au SW, Lam VM, Adams MJ Acta Crystallogr D Biol Crystallogr. 2005 May;61(Pt 5):495-504. Epub 2005, Apr 20. PMID:15858258<ref>PMID:15858258</ref>
-	~~[[2bh9]] 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=2BH9 OCA].~~	+

-	~~==Reference==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	<~~ref group="xtra"~~>~~PMID:015858258~~</~~ref~~>~~<ref group~~=~~"xtra">PMID:010745013</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 10:36, 24 March 2013

OCA — Sun, 24 Mar 2013 10:36:46 GMT

←Older revision		Revision as of 10:36, 24 March 2013
Line 1:		Line 1:
-	[[Image:2bh9.png\|left\|200px]]
-
-	<!--
-	The line below this paragraph, containing "STRUCTURE_2bh9", 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_2bh9\| PDB=2bh9 \| SCENE= }}		{{STRUCTURE_2bh9\| PDB=2bh9 \| SCENE= }}
-
	===X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP===		===X-RAY STRUCTURE OF A DELETION VARIANT OF HUMAN GLUCOSE 6-PHOSPHATE DEHYDROGENASE COMPLEXED WITH STRUCTURAL AND COENZYME NADP===
		+	{{ABSTRACT_PUBMED_15858258}}

		+	==Disease==
		+	[[http://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[http://omim.org/entry/305900 305900]]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>

-	~~<!--~~	+	==Function==
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_15858258}}, adds the Publication Abstract to the page~~	+	[[http://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.
-	~~(as it appears on PubMed at~~ http://www.~~pubmed~~.~~gov), where 15858258 is the PubMed ID number~~.	+
-	~~-->~~	+
-	~~{{ABSTRACT_PUBMED_15858258}}~~	+

	==About this Structure==		==About this Structure==
Line 22:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~15858258~~</ref><ref group="xtra">PMID:~~10745013~~</ref><~~ref~~ group="xtra"~~>PMID:10089300<~~/~~ref~~><references ~~group="xtra"~~/>	+	<ref group="xtra">PMID:015858258</ref><ref group="xtra">PMID:010745013</ref><references group="xtra"/><references/>
	[[Category: Glucose-6-phosphate dehydrogenase]]		[[Category: Glucose-6-phosphate dehydrogenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA: Protected "2bh9" [edit=sysop:move=sysop]

OCA — Mon, 14 Mar 2011 19:35:01 GMT

Protected "2bh9" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:35, 14 March 2011

OCA at 19:34, 14 March 2011

OCA — Mon, 14 Mar 2011 19:34:59 GMT

←Older revision		Revision as of 19:34, 14 March 2011
Line 1:		Line 1:
-	{{Seed}}
	[[Image:2bh9.png\|left\|200px]]		[[Image:2bh9.png\|left\|200px]]

Line 20:		Line 19:

	==About this Structure==		==About this Structure==
-	~~2BH9~~ 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=2BH9 OCA].	+	[[2bh9]] 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=2BH9 OCA].

	==Reference==		==Reference==
-	<ref group="xtra">PMID:15858258</ref><references group="xtra"/>	+	<ref group="xtra">PMID:15858258</ref><ref group="xtra">PMID:10745013</ref><ref group="xtra">PMID:10089300</ref><references group="xtra"/>
-	[[Category: Glucose-6-phosphate 1-dehydrogenase]]	+	[[Category: Glucose-6-phosphate dehydrogenase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Adams, M J.]]		[[Category: Adams, M J.]]
Line 32:		Line 31:
	[[Category: Carbohydrate metabolism]]		[[Category: Carbohydrate metabolism]]
	[[Category: Glucose metabolism]]		[[Category: Glucose metabolism]]
-		+	[[Category: Oxidoreductase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 20:39:59 2009''~~	+

←Older revision		Revision as of 10:31, 17 February 2021
Line 3:		Line 3:
	<StructureSection load='2bh9' size='340' side='right'caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>		<StructureSection load='2bh9' size='340' side='right'caption='[[2bh9]], [[Resolution\|resolution]] 2.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2bh9]] 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=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2bh9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BH9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BH9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qki\|1qki]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qki\|1qki]]</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-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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-6-phosphate_dehydrogenase Glucose-6-phosphate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.49 1.1.1.49] </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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [~~http~~://pdbe.org/2bh9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2bh9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2bh9 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=2bh9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bh9 OCA], [https://pdbe.org/2bh9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bh9 RCSB], [https://www.ebi.ac.uk/pdbsum/2bh9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bh9 ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[~~http~~://omim.org/entry/305900 305900]]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>	+	[[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) [MIM:[https://omim.org/entry/305900 305900]]. Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.<ref>PMID:1611091</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.	+	[[https://www.uniprot.org/uniprot/G6PD_HUMAN G6PD_HUMAN]] Produces pentose sugars for nucleic acid synthesis and main producer of NADPH reducing power.
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]