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| | <StructureSection load='1no3' size='340' side='right'caption='[[1no3]], [[Resolution|resolution]] 2.15Å' scene=''> | | <StructureSection load='1no3' size='340' side='right'caption='[[1no3]], [[Resolution|resolution]] 2.15Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1no3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_hispida Glycine hispida]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1byt 1byt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NO3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NO3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1no3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1byt 1byt]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NO3 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4NC:4-NITROCATECHOL'>4NC</scene>, <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]] 2.15Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1byt|1byt]], [[1n8q|1n8q]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4NC:4-NITROCATECHOL'>4NC</scene>, <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'>[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'>[https://proteopedia.org/fgij/fg.htm?mol=1no3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1no3 OCA], [https://pdbe.org/1no3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1no3 RCSB], [https://www.ebi.ac.uk/pdbsum/1no3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1no3 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=1no3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1no3 OCA], [http://pdbe.org/1no3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1no3 RCSB], [http://www.ebi.ac.uk/pdbsum/1no3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1no3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LOX3_SOYBN LOX3_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. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. | + | [https://www.uniprot.org/uniprot/LOX3_SOYBN LOX3_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. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Glycine hispida]] | + | [[Category: Glycine max]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Oxidoreductase]]
| + | [[Category: Borbulevych OY]] |
| - | [[Category: Borbulevych, O Y]] | + | [[Category: Jankun J]] |
| - | [[Category: Jankun, J]] | + | [[Category: Skrzypczak-Jankun E]] |
| - | [[Category: Skrzypczak-Jankun, E]] | + | |
| - | [[Category: 4-nitrocatechol]]
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| - | [[Category: Iron]]
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| - | [[Category: Lipoxygenase]]
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| Structural highlights
Function
LOX3_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. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
4-Nitrocatechol (4NC) is a known inhibitor of lipoxygenase. This work presents the X-ray structure of soybean lipoxygenase-3 in complex with 4NC refined at 2.15 A resolution. The X-ray analysis shows 4NC near iron with partial occupancy, blocking access to Fe but not covalently bound to it. The two hydroxyl groups interact with the C-terminus (4-OH) and His523 ND1 (3-OH). The residues surrounding the iron cofactor, His518*, His523, His709, Ile857* COO(-) and water, form a trigonal bipyramid with the residues marked with asterisks in the axial positions. The water bound to iron and the presence of the inhibitor seem to be responsible for the rearrangements and changes in the geometry of the ligand distribution and confirm the displacement of His518 from iron coordination. A description of the catechol binding contributes to the understanding of lipoxygenase inhibition and the participation of its co-oxidative activity in the utilization of natural flavonoids.
Soybean lipoxygenase-3 in complex with 4-nitrocatechol.,Skrzypczak-Jankun E, Borbulevych OY, Jankun J Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):613-5. Epub 2004, Feb 25. PMID:14993710[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Skrzypczak-Jankun E, Borbulevych OY, Jankun J. Soybean lipoxygenase-3 in complex with 4-nitrocatechol. Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):613-5. Epub 2004, Feb 25. PMID:14993710 doi:10.1107/S0907444904000861
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