3pzw - Revision history

OCA at 11:28, 14 March 2024

OCA — Thu, 14 Mar 2024 11:28:23 GMT

←Older revision		Revision as of 11:28, 14 March 2024
Line 10:		Line 10:
	== 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>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Determination of a macromolecular structure using x-ray diffraction is a multistep process that involves a plethora of techniques involving molecular biology, bioinformatics, and physical sciences. Counterintuitively, the success of any or all individual steps does not guarantee the success of the overall process. This review examines the difficulties presented by each step on the path from a gene to the final publication, together with certain lucky (or unlucky) circumstances that can affect the velocity along that path.
-
-	Determination of protein structures--a series of fortunate events.,Chruszcz M, Wlodawer A, Minor W Biophys J. 2008 Jul;95(1):1-9. Epub 2008 Apr 25. PMID:18441029<ref>PMID:18441029</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3pzw" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:46, 17 January 2024

OCA — Wed, 17 Jan 2024 12:46:23 GMT

←Older revision		Revision as of 12:46, 17 January 2024
Line 3:		Line 3:
	<StructureSection load='3pzw' size='340' side='right'caption='[[3pzw]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3pzw' size='340' side='right'caption='[[3pzw]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3pzw]] 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=3PZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3pzw]] 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=3PZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZW FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>~~, ~~<scene name='pdbligand=EDO:~~1~~,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</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='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1yge\|1yge]], [[1f8n\|1f8n]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">LOX1.~~1, ~~LOX1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine hispida])</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=3pzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzw OCA], [https://pdbe.org/3pzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pzw RCSB], [https://www.ebi.ac.uk/pdbsum/3pzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzw 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=3pzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzw OCA], [https://pdbe.org/3pzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pzw RCSB], [https://www.ebi.ac.uk/pdbsum/3pzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzw 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Glycine ~~hispida~~]]	+	[[Category: Glycine max]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Oxidoreductase]]~~	+	[[Category: Chruszcz M]]
-	[[Category: Chruszcz, M]]	+	[[Category: Minor W]]
-	[[Category: Minor, W]]	+
-	~~[[Category: Dioxygenase]]~~	+
-	~~[[Category: Lipoxygenase]]~~	+
-	~~[[Category: Metalloprotein~~]]	+

OCA at 09:57, 13 April 2022

OCA — Wed, 13 Apr 2022 09:57:15 GMT

←Older revision		Revision as of 09:57, 13 April 2022
Line 1:		Line 1:

	==Soybean lipoxygenase-1 - re-refinement==		==Soybean lipoxygenase-1 - re-refinement==
-	<StructureSection load='3pzw' size='340' side='right' caption='[[3pzw]], [[Resolution\|resolution]] 1.40Å' scene=''>	+	<StructureSection load='3pzw' size='340' side='right'caption='[[3pzw]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3pzw]] 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=3PZW OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3PZW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3pzw]] 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=3PZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PZW FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]]</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]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LOX1.1, LOX1 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine hispida])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LOX1.1, LOX1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine hispida])</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=3pzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzw OCA], [~~http~~://pdbe.org/3pzw PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3pzw RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3pzw PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzw 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=3pzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzw OCA], [https://pdbe.org/3pzw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3pzw RCSB], [https://www.ebi.ac.uk/pdbsum/3pzw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzw 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 26:
	</StructureSection>		</StructureSection>
	[[Category: Glycine hispida]]		[[Category: Glycine hispida]]
		+	[[Category: Large Structures]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]
	[[Category: Chruszcz, M]]		[[Category: Chruszcz, M]]

OCA at 08:32, 5 August 2016

OCA — Fri, 05 Aug 2016 08:32:08 GMT

←Older revision		Revision as of 08:32, 5 August 2016
Line 1:		Line 1:
		+
	==Soybean lipoxygenase-1 - re-refinement==		==Soybean lipoxygenase-1 - re-refinement==
	<StructureSection load='3pzw' size='340' side='right' caption='[[3pzw]], [[Resolution\|resolution]] 1.40Å' scene=''>		<StructureSection load='3pzw' size='340' side='right' caption='[[3pzw]], [[Resolution\|resolution]] 1.40Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3pzw]] 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=3PZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PZW FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3pzw]] 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=3PZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PZW FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LOX1.1, LOX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine ~~max~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LOX1.1, LOX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine hispida])</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=3pzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pzw RCSB], [http://www.ebi.ac.uk/pdbsum/3pzw 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=3pzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzw OCA], [http://pdbe.org/3pzw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3pzw RCSB], [http://www.ebi.ac.uk/pdbsum/3pzw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3pzw ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 3pzw" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Glycine ~~max~~]]	+	[[Category: Glycine hispida]]
-	[[Category: ~~Lipoxygenase~~]]	+	[[Category: Oxidoreductase]]
	[[Category: Chruszcz, M]]		[[Category: Chruszcz, M]]
	[[Category: Minor, W]]		[[Category: Minor, W]]
	[[Category: Dioxygenase]]		[[Category: Dioxygenase]]
		+	[[Category: Lipoxygenase]]
	[[Category: Metalloprotein]]		[[Category: Metalloprotein]]
-	[[Category: Oxidoreductase]]

OCA at 00:46, 25 December 2014

OCA — Thu, 25 Dec 2014 00:46:50 GMT

←Older revision		Revision as of 00:46, 25 December 2014
Line 9:		Line 9:
	<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=3pzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pzw RCSB], [http://www.ebi.ac.uk/pdbsum/3pzw 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=3pzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pzw RCSB], [http://www.ebi.ac.uk/pdbsum/3pzw 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>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 10:36, 19 December 2014

OCA — Fri, 19 Dec 2014 10:36:09 GMT

←Older revision		Revision as of 10:36, 19 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3pzw~~\| ~~PDB~~=3pzw \| ~~SCENE~~= }}	+	==Soybean lipoxygenase-1 - re-refinement==
-	===~~Soybean lipoxygenase~~-1 - re-~~refinement~~===	+	<StructureSection load='3pzw' size='340' side='right' caption='[[3pzw]], [[Resolution\|resolution]] 1.40Å' scene=''>
-	~~{{ABSTRACT_PUBMED_18441029}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3pzw]] 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=3PZW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3PZW FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1yge\|1yge]], [[1f8n\|1f8n]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LOX1.1, LOX1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3847 Glycine max])</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='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=3pzw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3pzw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3pzw RCSB], [http://www.ebi.ac.uk/pdbsum/3pzw PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Determination of a macromolecular structure using x-ray diffraction is a multistep process that involves a plethora of techniques involving molecular biology, bioinformatics, and physical sciences. Counterintuitively, the success of any or all individual steps does not guarantee the success of the overall process. This review examines the difficulties presented by each step on the path from a gene to the final publication, together with certain lucky (or unlucky) circumstances that can affect the velocity along that path.

-	~~==About this Structure==~~	+	Determination of protein structures--a series of fortunate events.,Chruszcz M, Wlodawer A, Minor W Biophys J. 2008 Jul;95(1):1-9. Epub 2008 Apr 25. PMID:18441029<ref>PMID:18441029</ref>
-	~~[[3pzw]] 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=3PZW OCA].~~	+

-	~~==Reference==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	<~~ref group="xtra"~~>~~PMID:018441029~~</~~ref~~>~~<ref group~~=~~"xtra">PMID:008718858</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Glycine max]]		[[Category: Glycine max]]
	[[Category: Lipoxygenase]]		[[Category: Lipoxygenase]]
-	[[Category: Chruszcz, M.]]	+	[[Category: Chruszcz, M]]
-	[[Category: Minor, W.]]	+	[[Category: Minor, W]]
	[[Category: Dioxygenase]]		[[Category: Dioxygenase]]
-	[[Category: Lipoxygenase]]
	[[Category: Metalloprotein]]		[[Category: Metalloprotein]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 08:35, 8 May 2013

OCA — Wed, 08 May 2013 08:35:01 GMT

←Older revision		Revision as of 08:35, 8 May 2013
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-	[[Image:3pzw.png\|left\|200px]]
-
-	<!--
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	{{STRUCTURE_3pzw\| PDB=3pzw \| SCENE= }}		{{STRUCTURE_3pzw\| PDB=3pzw \| SCENE= }}
-
	===Soybean lipoxygenase-1 - re-refinement===		===Soybean lipoxygenase-1 - re-refinement===
-
-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_18441029}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 18441029 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_18441029}}		{{ABSTRACT_PUBMED_18441029}}

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	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~18441029~~</ref><ref group="xtra">PMID:~~8718858~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:018441029</ref><ref group="xtra">PMID:008718858</ref><references group="xtra"/><references/>
	[[Category: Glycine max]]		[[Category: Glycine max]]
	[[Category: Lipoxygenase]]		[[Category: Lipoxygenase]]
	[[Category: Chruszcz, M.]]		[[Category: Chruszcz, M.]]
	[[Category: Minor, W.]]		[[Category: Minor, W.]]
		+	[[Category: Dioxygenase]]
		+	[[Category: Lipoxygenase]]
		+	[[Category: Metalloprotein]]
		+	[[Category: Oxidoreductase]]

OCA at 18:37, 14 March 2011

OCA — Mon, 14 Mar 2011 18:37:36 GMT

←Older revision		Revision as of 18:37, 14 March 2011
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-	[[Image:3pzw.~~jpg~~\|left\|200px]]	+	[[Image:3pzw.png\|left\|200px]]

	<!--		<!--

OCA: Protected "3pzw" [edit=sysop:move=sysop]

OCA — Wed, 19 Jan 2011 06:29:47 GMT

Protected "3pzw" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:29, 19 January 2011

OCA at 06:29, 19 January 2011

OCA — Wed, 19 Jan 2011 06:29:44 GMT

←Older revision		Revision as of 06:29, 19 January 2011
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-	~~'''Unreleased structure'''~~	+	[[Image:3pzw.jpg\|left\|200px]]

-	The ~~entry 3pzw~~ is ~~ON HOLD~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3pzw", 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_3pzw\| PDB=3pzw \| SCENE= }}

-	~~Authors: Chruszcz, M., Minor, W.~~	+	===Soybean lipoxygenase-1 - re-refinement===

-	Description: Soybean lipoxygenase-1 -re-refinement

-	~~''Page seeded by~~ [http://oca.weizmann.ac.il/oca OCA ] ~~on Wed Dec 22 09~~:38:~~42 2010''~~	+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_18441029}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 18441029 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_18441029}}
		+
		+	==About this Structure==
		+	[[3pzw]] 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=3PZW OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:18441029</ref><ref group="xtra">PMID:8718858</ref><references group="xtra"/>
		+	[[Category: Glycine max]]
		+	[[Category: Lipoxygenase]]
		+	[[Category: Chruszcz, M.]]
		+	[[Category: Minor, W.]]