3pzw
From Proteopedia
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| - | {{STRUCTURE_3pzw| PDB=3pzw | SCENE= }} | ||
| - | ===Soybean lipoxygenase-1 - re-refinement=== | ||
| - | {{ABSTRACT_PUBMED_18441029}} | ||
| - | == | + | ==Soybean lipoxygenase-1 - re-refinement== |
| - | [[3pzw]] is a 1 chain structure with sequence from [ | + | <StructureSection load='3pzw' size='340' side='right'caption='[[3pzw]], [[Resolution|resolution]] 1.40Å' scene=''> |
| - | + | == Structural highlights == | |
| - | == | + | <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='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='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='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> | ||
| + | == 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> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Chruszcz | + | [[Category: Chruszcz M]] |
| - | [[Category: Minor | + | [[Category: Minor W]] |
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Current revision
Soybean lipoxygenase-1 - re-refinement
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