5tqp
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==LIPOXYGENASE-1 (SOYBEAN) I553G MUTANT AT 300K== | |
| - | + | <StructureSection load='5tqp' size='340' side='right' caption='[[5tqp]], [[Resolution|resolution]] 1.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[5tqp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TQP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TQP 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> | |
| - | [[Category: | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tqo|5tqo]], [[5tqn|5tqn]], [[5tr0|5tr0]]</td></tr> |
| - | [[Category: Poss, E | + | <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> |
| - | [[Category: | + | <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=5tqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tqp OCA], [http://pdbe.org/5tqp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tqp RCSB], [http://www.ebi.ac.uk/pdbsum/5tqp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tqp ProSAT]</span></td></tr> |
| + | </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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Fraser, J S]] | ||
| + | [[Category: Poss, E M]] | ||
| + | [[Category: Hydrogen tunneling]] | ||
| + | [[Category: Lipoxygenase]] | ||
Revision as of 06:30, 1 November 2017
LIPOXYGENASE-1 (SOYBEAN) I553G MUTANT AT 300K
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