5lbz - Revision history

OCA at 08:55, 11 October 2023

OCA — Wed, 11 Oct 2023 08:55:46 GMT

←Older revision		Revision as of 08:55, 11 October 2023
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	==Structure of the human quinone reductase 2 (NQO2) in complex with pacritinib==		==Structure of the human quinone reductase 2 (NQO2) in complex with pacritinib==
-	<StructureSection load='5lbz' size='340' side='right' caption='[[5lbz]], [[Resolution\|resolution]] 1.40Å' scene=''>	+	<StructureSection load='5lbz' size='340' side='right'caption='[[5lbz]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lbz]] is a 2 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=5LBZ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5LBZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lbz]] is a 2 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=5LBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LBZ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6T3:11-(2-pyrrolidin-1-yl-ethoxy)-14,19-dioxa-5,7,26-triaza-tetracyclo[19.3.1.1(2,6).1(8,12)]heptacosa-1(25),2(26),3,5,8,10,12(27),16,21,23-decaene'>6T3</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.4Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NQO2, NMOR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=6T3:11-(2-pyrrolidin-1-yl-ethoxy)-14,19-dioxa-5,7,26-triaza-tetracyclo[19.3.1.1(2,6).1(8,12)]heptacosa-1(25),2(26),3,5,8,10,12(27),16,21,23-decaene'>6T3</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribosyldihydronicotinamide_dehydrogenase_(quinone) Ribosyldihydronicotinamide dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.5.1 1.10.5.1] </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=5lbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbz OCA], [https://pdbe.org/5lbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lbz RCSB], [https://www.ebi.ac.uk/pdbsum/5lbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbz ProSAT]</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=5lbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbz OCA], [~~http~~://pdbe.org/5lbz PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5lbz RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5lbz PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbz ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/NQO2_HUMAN NQO2_HUMAN]] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.<ref>PMID:18254726</ref>	+	[https://www.uniprot.org/uniprot/NQO2_HUMAN NQO2_HUMAN] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.<ref>PMID:18254726</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 5lbz" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 5lbz" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Quinone reductase 3D structures\|Quinone reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Kuster, B~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Medard, G~~]]	+	[[Category: Kuster B]]
-	[[Category: ~~Schneider, S~~]]	+	[[Category: Medard G]]
-	[[Category: ~~Kinase inhibitor]]~~	+	[[Category: Schneider S]]
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Pancritinib]]~~	+
-	~~[[Category: Quinone reductase 2~~]]	+

OCA at 07:25, 13 December 2017

OCA — Wed, 13 Dec 2017 07:25:49 GMT

←Older revision		Revision as of 07:25, 13 December 2017
Line 11:		Line 11:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/NQO2_HUMAN NQO2_HUMAN]] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.<ref>PMID:18254726</ref>		[[http://www.uniprot.org/uniprot/NQO2_HUMAN NQO2_HUMAN]] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.<ref>PMID:18254726</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Kinase inhibitors are important cancer therapeutics. Polypharmacology is commonly observed, requiring thorough target deconvolution to understand drug mechanism of action. Using chemical proteomics, we analyzed the target spectrum of 243 clinically evaluated kinase drugs. The data revealed previously unknown targets for established drugs, offered a perspective on the "druggable" kinome, highlighted (non)kinase off-targets, and suggested potential therapeutic applications. Integration of phosphoproteomic data refined drug-affected pathways, identified response markers, and strengthened rationale for combination treatments. We exemplify translational value by discovering SIK2 (salt-inducible kinase 2) inhibitors that modulate cytokine production in primary cells, by identifying drugs against the lung cancer survival marker MELK (maternal embryonic leucine zipper kinase), and by repurposing cabozantinib to treat FLT3-ITD-positive acute myeloid leukemia. This resource, available via the ProteomicsDB database, should facilitate basic, clinical, and drug discovery research and aid clinical decision-making.
		+
		+	The target landscape of clinical kinase drugs.,Klaeger S, Heinzlmeir S, Wilhelm M, Polzer H, Vick B, Koenig PA, Reinecke M, Ruprecht B, Petzoldt S, Meng C, Zecha J, Reiter K, Qiao H, Helm D, Koch H, Schoof M, Canevari G, Casale E, Depaolini SR, Feuchtinger A, Wu Z, Schmidt T, Rueckert L, Becker W, Huenges J, Garz AK, Gohlke BO, Zolg DP, Kayser G, Vooder T, Preissner R, Hahne H, Tonisson N, Kramer K, Gotze K, Bassermann F, Schlegl J, Ehrlich HC, Aiche S, Walch A, Greif PA, Schneider S, Felder ER, Ruland J, Medard G, Jeremias I, Spiekermann K, Kuster B Science. 2017 Dec 1;358(6367). pii: 358/6367/eaan4368. doi:, 10.1126/science.aan4368. PMID:29191878<ref>PMID:29191878</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5lbz" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 07:39, 6 December 2017

OCA — Wed, 06 Dec 2017 07:39:19 GMT

←Older revision		Revision as of 07:39, 6 December 2017
Line 3:		Line 3:
	<StructureSection load='5lbz' size='340' side='right' caption='[[5lbz]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='5lbz' size='340' side='right' caption='[[5lbz]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5lbz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LBZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LBZ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5lbz]] is a 2 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=5LBZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LBZ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6T3:11-(2-pyrrolidin-1-yl-ethoxy)-14,19-dioxa-5,7,26-triaza-tetracyclo[19.3.1.1(2,6).1(8,12)]heptacosa-1(25),2(26),3,5,8,10,12(27),16,21,23-decaene'>6T3</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6T3:11-(2-pyrrolidin-1-yl-ethoxy)-14,19-dioxa-5,7,26-triaza-tetracyclo[19.3.1.1(2,6).1(8,12)]heptacosa-1(25),2(26),3,5,8,10,12(27),16,21,23-decaene'>6T3</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">NQO2, NMOR2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribosyldihydronicotinamide_dehydrogenase_(quinone) Ribosyldihydronicotinamide dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.5.1 1.10.5.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribosyldihydronicotinamide_dehydrogenase_(quinone) Ribosyldihydronicotinamide dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.5.1 1.10.5.1] </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=5lbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbz OCA], [http://pdbe.org/5lbz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lbz RCSB], [http://www.ebi.ac.uk/pdbsum/5lbz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbz ProSAT]</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=5lbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbz OCA], [http://pdbe.org/5lbz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lbz RCSB], [http://www.ebi.ac.uk/pdbsum/5lbz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbz ProSAT]</span></td></tr>
Line 14:		Line 15:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Kuster, B]]		[[Category: Kuster, B]]
	[[Category: Medard, G]]		[[Category: Medard, G]]

OCA at 06:05, 29 November 2017

OCA — Wed, 29 Nov 2017 06:05:52 GMT

←Older revision		Revision as of 06:05, 29 November 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 5lbz is ~~ON HOLD~~	+	==Structure of the human quinone reductase 2 (NQO2) in complex with pacritinib==
-		+	<StructureSection load='5lbz' size='340' side='right' caption='[[5lbz]], [[Resolution\|resolution]] 1.40Å' scene=''>
-	~~Authors~~: ~~Schneider~~, S., ~~Medard~~, G., ~~Kuster~~, B.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5lbz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LBZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LBZ FirstGlance]. <br>
-	~~Description~~: ~~Structure of the human~~ quinone reductase ~~2 (NQO2)~~ in ~~complex~~ with ~~pacritinib~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6T3:11-(2-pyrrolidin-1-yl-ethoxy)-14,19-dioxa-5,7,26-triaza-tetracyclo[19.3.1.1(2,6).1(8,12)]heptacosa-1(25),2(26),3,5,8,10,12(27),16,21,23-decaene'>6T3</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribosyldihydronicotinamide_dehydrogenase_(quinone) Ribosyldihydronicotinamide dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.5.1 1.10.5.1] </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=5lbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lbz OCA], [http://pdbe.org/5lbz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lbz RCSB], [http://www.ebi.ac.uk/pdbsum/5lbz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lbz ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/NQO2_HUMAN NQO2_HUMAN]] The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.<ref>PMID:18254726</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Kuster, B]]
	[[Category: Medard, G]]		[[Category: Medard, G]]
	[[Category: Schneider, S]]		[[Category: Schneider, S]]
-	[[Category: ~~Kuster, B~~]]	+	[[Category: Kinase inhibitor]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Pancritinib]]
		+	[[Category: Quinone reductase 2]]

OCA: Protected "5lbz" [edit=sysop:move=sysop]

OCA — Wed, 13 Jul 2016 00:56:12 GMT

Protected "5lbz" [edit=sysop:move=sysop]

←Older revision

Revision as of 00:56, 13 July 2016

OCA: New page: '''Unreleased structure''' The entry 5lbz is ON HOLD Authors: Schneider, S., Medard, G., Kuster, B. Description: Structure of the human quinone reductase 2 (NQO2) in complex with pacri...

OCA — Wed, 13 Jul 2016 00:56:11 GMT

New page: '''Unreleased structure''' The entry 5lbz is ON HOLD Authors: Schneider, S., Medard, G., Kuster, B. Description: Structure of the human quinone reductase 2 (NQO2) in complex with pacri...

New page

'''Unreleased structure'''

The entry 5lbz is ON HOLD

Authors: Schneider, S., Medard, G., Kuster, B.

Description: Structure of the human quinone reductase 2 (NQO2) in complex with pacritinib
[[Category: Unreleased Structures]]
[[Category: Medard, G]]
[[Category: Schneider, S]]
[[Category: Kuster, B]]