4qof - Revision history

OCA at 17:34, 20 September 2023

2023-09-20T17:34:16Z

←Older revision		Revision as of 17:34, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4qof]] 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=4QOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QOF FirstGlance]. <br>		<table><tr><td colspan='2'>[[4qof]] 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=4QOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QOF FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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]] 1.55Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qof OCA], [https://pdbe.org/4qof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qof RCSB], [https://www.ebi.ac.uk/pdbsum/4qof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qof 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=4qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qof OCA], [https://pdbe.org/4qof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qof RCSB], [https://www.ebi.ac.uk/pdbsum/4qof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qof ProSAT]</span></td></tr>
	</table>		</table>

OCA at 13:43, 22 February 2023

2023-02-22T13:43:54Z

←Older revision		Revision as of 13:43, 22 February 2023
Line 3:		Line 3:
	<StructureSection load='4qof' size='340' side='right'caption='[[4qof]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='4qof' size='340' side='right'caption='[[4qof]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4qof]] 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=4QOF OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4QOF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4qof]] 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=4QOF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QOF FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qof OCA], [https://pdbe.org/4qof PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qof RCSB], [https://www.ebi.ac.uk/pdbsum/4qof PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qof ProSAT]</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=1.10.99.2 1.10.99.2] </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=4qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qof OCA], [~~http~~://pdbe.org/4qof PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4qof RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4qof PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4qof 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;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Melatonin exerts its biological effects through at least two transmembrane G-protein-coupled receptors, MT1 and MT2, and a lower-affinity cytosolic binding site, designated MT3. MT3 has recently been identified as QR2 (quinone reductase 2) (EC 1.10.99.2) which is of significance since it links the antioxidant effects of melatonin to a mechanism of action. Initially, QR2 was believed to function analogously to QR1 in protecting cells from highly reactive quinones. However, recent studies indicate that QR2 may actually transform certain quinone substrates into more highly reactive compounds capable of causing cellular damage. Therefore it is hypothesized that inhibition of QR2 in certain cases may lead to protection of cells against these highly reactive species. Since melatonin is known to inhibit QR2 activity, but its binding site and mode of inhibition are not known, we determined the mechanism of inhibition of QR2 by melatonin and a series of melatonin and 5-hydroxytryptamine (serotonin) analogues, and we determined the X-ray structures of melatonin and 2-iodomelatonin in complex with QR2 to between 1.5 and 1.8 A (1 A=0.1 nm) resolution. Finally, the thermodynamic binding constants for melatonin and 2-iodomelatonin were determined by ITC (isothermal titration calorimetry). The kinetic results indicate that melatonin is a competitive inhibitor against N-methyldihydronicotinamide (K(i)=7.2 microM) and uncompetitive against menadione (K(i)=92 microM), and the X-ray structures shows that melatonin binds in multiple orientations within the active sites of the QR2 dimer as opposed to an allosteric site. These results provide new insights into the binding mechanisms of melatonin and analogues to QR2.	+

-	Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2.,Calamini B, Santarsiero BD, Boutin JA, Mesecar AD Biochem J. 2008 Jul 1;413(1):81-91. PMID:18254726<ref>PMID:18254726</ref>	+	==See Also==
-		+	*[[Quinone reductase\|Quinone reductase]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class~~=~~"pdbe-citations 4qof" style~~=~~"background-color:#fffaf0;"></div>~~	+
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Antoine, M]]	+	[[Category: Antoine M]]
-	[[Category: Boutin~~, J A~~]]	+	[[Category: Boutin JA]]
-	[[Category: Ferry, G]]	+	[[Category: Ferry G]]
-	[[Category: Isabet, T]]	+	[[Category: Isabet T]]
-	[[Category: Serriere, J]]	+	[[Category: Serriere J]]
-	~~[[Category: Flavin mononucleotide]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Oxidoreductase flavoprotein~~]]	+

OCA at 08:44, 24 April 2019

2019-04-24T08:44:51Z

←Older revision		Revision as of 08:44, 24 April 2019
Line 1:		Line 1:

	==Crystal structure of fmn quinone reductase 2 AT 1.55A==		==Crystal structure of fmn quinone reductase 2 AT 1.55A==
-	<StructureSection load='4qof' size='340' side='right' caption='[[4qof]], [[Resolution\|resolution]] 1.55Å' scene=''>	+	<StructureSection load='4qof' size='340' side='right'caption='[[4qof]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4qof]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QOF FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4qof]] 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=4QOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QOF FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=1.10.99.2 1.10.99.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribosyldihydronicotinamide_dehydrogenase_(quinone) Ribosyldihydronicotinamide dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.99.2 1.10.99.2] </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=4qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qof OCA], [http://pdbe.org/4qof PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qof RCSB], [http://www.ebi.ac.uk/pdbsum/4qof PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qof 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=4qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qof OCA], [http://pdbe.org/4qof PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qof RCSB], [http://www.ebi.ac.uk/pdbsum/4qof PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qof ProSAT]</span></td></tr>
Line 23:		Line 24:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Antoine, M]]		[[Category: Antoine, M]]
	[[Category: Boutin, J A]]		[[Category: Boutin, J A]]

OCA at 13:46, 5 April 2017

2017-04-05T13:46:30Z

←Older revision		Revision as of 13:46, 5 April 2017
Line 1:		Line 1:
		+
	==Crystal structure of fmn quinone reductase 2 AT 1.55A==		==Crystal structure of fmn quinone reductase 2 AT 1.55A==
	<StructureSection load='4qof' size='340' side='right' caption='[[4qof]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='4qof' size='340' side='right' caption='[[4qof]], [[Resolution\|resolution]] 1.55Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=1.10.99.2 1.10.99.2] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribosyldihydronicotinamide_dehydrogenase_(quinone) Ribosyldihydronicotinamide dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.99.2 1.10.99.2] </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=4qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qof RCSB], [http://www.ebi.ac.uk/pdbsum/4qof 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=4qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qof OCA], [http://pdbe.org/4qof PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qof RCSB], [http://www.ebi.ac.uk/pdbsum/4qof PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qof ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4qof" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:10, 1 July 2015

2015-07-01T12:10:18Z

←Older revision		Revision as of 12:10, 1 July 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of fmn quinone reductase 2 AT 1.55A==
		+	<StructureSection load='4qof' size='340' side='right' caption='[[4qof]], [[Resolution\|resolution]] 1.55Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4qof]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QOF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QOF FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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=1.10.99.2 1.10.99.2] </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=4qof FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qof OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qof RCSB], [http://www.ebi.ac.uk/pdbsum/4qof PDBsum]</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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Melatonin exerts its biological effects through at least two transmembrane G-protein-coupled receptors, MT1 and MT2, and a lower-affinity cytosolic binding site, designated MT3. MT3 has recently been identified as QR2 (quinone reductase 2) (EC 1.10.99.2) which is of significance since it links the antioxidant effects of melatonin to a mechanism of action. Initially, QR2 was believed to function analogously to QR1 in protecting cells from highly reactive quinones. However, recent studies indicate that QR2 may actually transform certain quinone substrates into more highly reactive compounds capable of causing cellular damage. Therefore it is hypothesized that inhibition of QR2 in certain cases may lead to protection of cells against these highly reactive species. Since melatonin is known to inhibit QR2 activity, but its binding site and mode of inhibition are not known, we determined the mechanism of inhibition of QR2 by melatonin and a series of melatonin and 5-hydroxytryptamine (serotonin) analogues, and we determined the X-ray structures of melatonin and 2-iodomelatonin in complex with QR2 to between 1.5 and 1.8 A (1 A=0.1 nm) resolution. Finally, the thermodynamic binding constants for melatonin and 2-iodomelatonin were determined by ITC (isothermal titration calorimetry). The kinetic results indicate that melatonin is a competitive inhibitor against N-methyldihydronicotinamide (K(i)=7.2 microM) and uncompetitive against menadione (K(i)=92 microM), and the X-ray structures shows that melatonin binds in multiple orientations within the active sites of the QR2 dimer as opposed to an allosteric site. These results provide new insights into the binding mechanisms of melatonin and analogues to QR2.

-	~~The entry 4qof is ON HOLD until Paper Publication~~	+	Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2.,Calamini B, Santarsiero BD, Boutin JA, Mesecar AD Biochem J. 2008 Jul 1;413(1):81-91. PMID:18254726<ref>PMID:18254726</ref>

-	~~Authors: Serriere~~, J.~~, Boutin, J~~.A.~~, Isabet, T.,~~ Antoine, M~~., Ferry, G.~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Crystal structure of fmn quinone reductase 2 AT 1.55A~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Antoine, M]]
		+	[[Category: Boutin, J A]]
	[[Category: Ferry, G]]		[[Category: Ferry, G]]
-	[[Category: ~~Antoine~~, M]]	+	[[Category: Isabet, T]]
	[[Category: Serriere, J]]		[[Category: Serriere, J]]
-	[[Category: ~~Isabet, T~~]]	+	[[Category: Flavin mononucleotide]]
-	[[Category: ~~Boutin, J.A~~]]	+	[[Category: Oxidoreductase]]
		+	[[Category: Oxidoreductase flavoprotein]]

OCA at 15:59, 24 December 2014

2014-12-24T15:59:00Z

←Older revision		Revision as of 15:59, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of fmn quinone reductase 2 AT 1.55A		Description: Crystal structure of fmn quinone reductase 2 AT 1.55A
		+	[[Category: Unreleased Structures]]
		+	[[Category: Ferry, G]]
		+	[[Category: Antoine, M]]
		+	[[Category: Serriere, J]]
		+	[[Category: Isabet, T]]
		+	[[Category: Boutin, J.A]]

OCA at 11:20, 19 November 2014

2014-11-19T11:20:50Z

←Older revision		Revision as of 11:20, 19 November 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4qof is ON HOLD	+	The entry 4qof is ON HOLD until Paper Publication

	Authors: Serriere, J., Boutin, J.A., Isabet, T., Antoine, M., Ferry, G.		Authors: Serriere, J., Boutin, J.A., Isabet, T., Antoine, M., Ferry, G.

	Description: Crystal structure of fmn quinone reductase 2 AT 1.55A		Description: Crystal structure of fmn quinone reductase 2 AT 1.55A

OCA at 14:38, 20 August 2014

2014-08-20T14:38:04Z

←Older revision		Revision as of 14:38, 20 August 2014
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	Authors: Serriere, J., Boutin, J.A., Isabet, T., Antoine, M., Ferry, G.		Authors: Serriere, J., Boutin, J.A., Isabet, T., Antoine, M., Ferry, G.

-	Description: ~~CRYSTAL STRUCTURE OF FMN QUINONE REDUCTASE~~ 2 AT 1.55A	+	Description: Crystal structure of fmn quinone reductase 2 AT 1.55A

OCA: Protected "4qof" [edit=sysop:move=sysop]

2014-07-02T07:25:32Z

Protected "4qof" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:25, 2 July 2014

OCA: New page: '''Unreleased structure''' The entry 4qof is ON HOLD Authors: Serriere, J., Boutin, J.A., Isabet, T., Antoine, M., Ferry, G. Description: CRYSTAL STRUCTURE OF FMN QUINONE REDUCTASE 2 A...

2014-07-02T07:25:31Z

New page: '''Unreleased structure''' The entry 4qof is ON HOLD Authors: Serriere, J., Boutin, J.A., Isabet, T., Antoine, M., Ferry, G. Description: CRYSTAL STRUCTURE OF FMN QUINONE REDUCTASE 2 A...

New page

'''Unreleased structure'''

The entry 4qof is ON HOLD

Authors: Serriere, J., Boutin, J.A., Isabet, T., Antoine, M., Ferry, G.

Description: CRYSTAL STRUCTURE OF FMN QUINONE REDUCTASE 2 AT 1.55A