1fgq - Revision history

OCA at 06:03, 9 August 2023

2023-08-09T06:03:46Z

←Older revision		Revision as of 06:03, 9 August 2023
Line 3:		Line 3:
	<StructureSection load='1fgq' size='340' side='right'caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='1fgq' size='340' side='right'caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Glycine_hispida~~ Glycine ~~hispida~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=FE:FE+(III)+ION'>FE</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]] 1.85Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style='overflow: auto; max-height: 3em;'>[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</div></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
-	~~<tr~~ id~~='activity'><td class~~="~~sblockLbl~~"><~~b>Activity:</b></td><td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12]~~ </~~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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [https://pdbe.org/1fgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [https://www.ebi.ac.uk/pdbsum/1fgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgq 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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [https://pdbe.org/1fgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [https://www.ebi.ac.uk/pdbsum/1fgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/LOX1_SOYBN LOX1_SOYBN]] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.<ref>PMID:16157595</ref>	+	[https://www.uniprot.org/uniprot/LOX1_SOYBN LOX1_SOYBN] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.<ref>PMID:16157595</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 34:		Line 33:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Glycine ~~hispida~~]]	+	[[Category: Glycine max]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Oxidoreductase]]~~	+	[[Category: Holman T]]
-	[[Category: Holman, T]]	+	[[Category: Minor W]]
-	[[Category: Minor, W]]	+	[[Category: Tomchick DR]]
-	[[Category: Tomchick~~, D R]]~~	+
-	~~[[Category: Dioxygenase]]~~	+
-	~~[[Category: Fatty acid]]~~	+
-	~~[[Category: Lipoxygenase]]~~	+
-	~~[[Category: Metalloprotein~~]]	+

OCA at 11:09, 28 July 2021

2021-07-28T11:09:23Z

←Older revision		Revision as of 11:09, 28 July 2021
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	<StructureSection load='1fgq' size='340' side='right'caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='1fgq' size='340' side='right'caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [~~http~~://pdbe.org/1fgq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1fgq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgq 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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [https://pdbe.org/1fgq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [https://www.ebi.ac.uk/pdbsum/1fgq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/LOX1_SOYBN LOX1_SOYBN]] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.<ref>PMID:16157595</ref>	+	[[https://www.uniprot.org/uniprot/LOX1_SOYBN LOX1_SOYBN]] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.<ref>PMID:16157595</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 08:53, 23 October 2019

2019-10-23T08:53:16Z

←Older revision		Revision as of 08:53, 23 October 2019
Line 1:		Line 1:

	==LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495E MUTANT==		==LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495E MUTANT==
-	<StructureSection load='1fgq' size='340' side='right' caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>	+	<StructureSection load='1fgq' size='340' side='right'caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>
Line 35:		Line 35:
	</StructureSection>		</StructureSection>
	[[Category: Glycine hispida]]		[[Category: Glycine hispida]]
		+	[[Category: Large Structures]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Holman, T]]		[[Category: Holman, T]]

OCA at 09:19, 27 December 2017

2017-12-27T09:19:59Z

←Older revision		Revision as of 09:19, 27 December 2017
Line 1:		Line 1:
		+
	==LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495E MUTANT==		==LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495E MUTANT==
	<StructureSection load='1fgq' size='340' side='right' caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='1fgq' size='340' side='right' caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [http://pdbe.org/1fgq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [http://www.ebi.ac.uk/pdbsum/1fgq 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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [http://pdbe.org/1fgq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [http://www.ebi.ac.uk/pdbsum/1fgq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgq ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
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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/fg/1fgq_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fg/1fgq_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>

OCA at 01:40, 10 February 2016

2016-02-10T01:40:24Z

←Older revision		Revision as of 01:40, 10 February 2016
Line 18:		Line 18:
	<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=1fgq ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 04:06, 11 September 2015

2015-09-11T04:06:22Z

←Older revision		Revision as of 04:06, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1fgq' size='340' side='right' caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='1fgq' size='340' side='right' caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Glycine_max~~ Glycine ~~max~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Lipoxygenase Lipoxygenase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [http://www.ebi.ac.uk/pdbsum/1fgq 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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [http://pdbe.org/1fgq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [http://www.ebi.ac.uk/pdbsum/1fgq PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 28:		Line 28:
	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 1fgq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Glycine ~~max~~]]	+	[[Category: Glycine hispida]]
-	[[Category: ~~Lipoxygenase~~]]	+	[[Category: Oxidoreductase]]
	[[Category: Holman, T]]		[[Category: Holman, T]]
	[[Category: Minor, W]]		[[Category: Minor, W]]
Line 39:		Line 40:
	[[Category: Dioxygenase]]		[[Category: Dioxygenase]]
	[[Category: Fatty acid]]		[[Category: Fatty acid]]
		+	[[Category: Lipoxygenase]]
	[[Category: Metalloprotein]]		[[Category: Metalloprotein]]
-	[[Category: Oxidoreductase]]

OCA at 10:54, 25 December 2014

2014-12-25T10:54:58Z

←Older revision		Revision as of 10:54, 25 December 2014
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	<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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [http://www.ebi.ac.uk/pdbsum/1fgq 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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [http://www.ebi.ac.uk/pdbsum/1fgq PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LOX1_SOYBN LOX1_SOYBN]] Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.<ref>PMID:16157595</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 00:29, 23 December 2014

2014-12-23T00:29:35Z

←Older revision		Revision as of 00:29, 23 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [http://www.ebi.ac.uk/pdbsum/1fgq 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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [http://www.ebi.ac.uk/pdbsum/1fgq PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 32:		Line 32:
	[[Category: Glycine max]]		[[Category: Glycine max]]
	[[Category: Lipoxygenase]]		[[Category: Lipoxygenase]]
-	[[Category: Holman, T.]]	+	[[Category: Holman, T]]
-	[[Category: Minor, W.]]	+	[[Category: Minor, W]]
-	[[Category: Tomchick, D R.]]	+	[[Category: Tomchick, D R]]
	[[Category: Dioxygenase]]		[[Category: Dioxygenase]]
	[[Category: Fatty acid]]		[[Category: Fatty acid]]
-	[[Category: Lipoxygenase]]
	[[Category: Metalloprotein]]		[[Category: Metalloprotein]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA: Protected "1fgq" [edit=sysop:move=sysop]

2014-09-28T14:18:08Z

Protected "1fgq" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:18, 28 September 2014

OCA at 14:18, 28 September 2014

2014-09-28T14:18:06Z

←Older revision		Revision as of 14:18, 28 September 2014
Line 1:		Line 1:
-	~~{{Seed}}~~	+	==LIPOXYGENASE-1 (SOYBEAN) AT 100K, Q495E MUTANT==
-	[[~~Image:~~1fgq.~~png~~\|~~left~~\|200px]]	+	<StructureSection load='1fgq' size='340' side='right' caption='[[1fgq]], [[Resolution\|resolution]] 1.85Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1fgq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FGQ FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]], [[1fgm\|1fgm]], [[1fgo\|1fgo]], [[1fgr\|1fgr]], [[1fgt\|1fgt]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lipoxygenase Lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.12 1.13.11.12] </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=1fgq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1fgq RCSB], [http://www.ebi.ac.uk/pdbsum/1fgq PDBsum]</span></td></tr>
		+	<table>
		+	== 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/fg/1fgq_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 ==
		+	Lipoxygenases are an important class of non-heme iron enzymes that catalyze the hydroperoxidation of unsaturated fatty acids. The details of the enzymatic mechanism of lipoxygenases are still not well understood. This study utilizes a combination of kinetic and structural probes to relate the lipoxygenase mechanism of action with structural modifications of the iron's second coordination sphere. The second coordination sphere consists of Gln(495) and Gln(697), which form a hydrogen bond network between the substrate cavity and the first coordination sphere (Asn(694)). In this investigation, we compared the kinetic and structural properties of four mutants (Q495E, Q495A, Q697N, and Q697E) with those of wild-type soybean lipoxygenase-1 and determined that changes in the second coordination sphere affected the enzymatic activity by hydrogen bond rearrangement and substrate positioning through interaction with Gln(495). The nature of the C-H bond cleavage event remained unchanged, which demonstrates that the mutations have not affected the mechanism of hydrogen atom tunneling. The unusual and dramatic inverse solvent isotope effect (SIE) observed for the Q697E mutant indicated that an Fe(III)-OH(-) is the active site base. A new transition state model for hydrogen atom abstraction is proposed.

-	<!--	+	Structural and functional characterization of second-coordination sphere mutants of soybean lipoxygenase-1.,Tomchick DR, Phan P, Cymborowski M, Minor W, Holman TR Biochemistry. 2001 Jun 26;40(25):7509-17. PMID:11412104<ref>PMID:11412104</ref>
-	~~The line below this paragraph~~, ~~containing "STRUCTURE_1fgq"~~, ~~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_1fgq\| PDB=1fgq \| SCENE= }}~~	+

-	~~===LIPOXYGENASE-1 (SOYBEAN) AT 100K~~, ~~Q495E MUTANT===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	~~<!--~~	+	<references/>
-	~~The line below this paragraph, {{ABSTRACT_PUBMED_11412104}}, adds~~ the ~~Publication Abstract to the page~~	+	__TOC__
-	~~(as it appears on PubMed at http://www~~.~~pubmed~~.~~gov), where 11412104 is the PubMed ID number~~.	+	</StructureSection>
-	-->	+
-	~~{{ABSTRACT_PUBMED_11412104}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~1FGQ is a 1 chain structure of sequence from [http:~~/~~/en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGQ OCA].~~	+
-		+
-	==~~Reference~~==	+
-	<~~ref group="xtra">PMID:11412104<~~/~~ref~~><~~references group="xtra"~~/>	+
	[[Category: Glycine max]]		[[Category: Glycine max]]
	[[Category: Lipoxygenase]]		[[Category: Lipoxygenase]]
Line 33:		Line 39:
	[[Category: Lipoxygenase]]		[[Category: Lipoxygenase]]
	[[Category: Metalloprotein]]		[[Category: Metalloprotein]]
-		+	[[Category: Oxidoreductase]]
-	~~''Page seeded by~~ [~~http~~:~~//oca.weizmann.ac.il/oca OCA~~ ] ~~on Tue Feb 17 14:23:19 2009''~~	+