5t5v: Difference between revisions
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<StructureSection load='5t5v' size='340' side='right' caption='[[5t5v]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='5t5v' size='340' side='right' caption='[[5t5v]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5t5v]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T5V FirstGlance]. <br> | <table><tr><td colspan='2'>[[5t5v]] is a 2 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=5T5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T5V 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='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/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=5t5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5v OCA], [http://pdbe.org/5t5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t5v RCSB], [http://www.ebi.ac.uk/pdbsum/5t5v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5v 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=5t5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t5v OCA], [http://pdbe.org/5t5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t5v RCSB], [http://www.ebi.ac.uk/pdbsum/5t5v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t5v ProSAT]</span></td></tr> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Glycine hispida]] | |||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Fraser, J S]] | [[Category: Fraser, J S]] | ||
Revision as of 17:21, 6 November 2017
LIPOXYGENASE-1 (SOYBEAN) AT 293KLIPOXYGENASE-1 (SOYBEAN) AT 293K
Structural highlights
Function[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.[1] References
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