5tr0: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5tr0 is ~~ON HOLD until Paper Publication~~

==Lipoxygenase-1 (soybean) L754A mutant at 293K==

~~Authors~~: ~~Poss~~, E.M., ~~Fraser~~, J.S.

== Structural highlights ==

<table><tr><td colspan='2'>[[5tr0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TR0 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TR0 FirstGlance].

~~Description~~: ~~Lipoxygenase~~-1 (~~soybean~~) ~~L754A mutant~~ at ~~293K~~

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<tr id='related'><td class="sblockLbl">[[Related_structure|Related:]]</td><td class="sblockDat">[[5tqn|5tqn]], [[5tqp|5tqp]], [[5tqo|5tqo]]</td></tr>

[[Category: Poss, E.M]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

[[Category: ~~Fraser, J.S~~]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5tr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tr0 OCA], [http://pdbe.org/5tr0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tr0 RCSB], [http://www.ebi.ac.uk/pdbsum/5tr0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tr0 ProSAT]</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 ==

__TOC__

</StructureSection>

[[Category: Oxidoreductase]]

[[Category: Fraser, J S]]

[[Category: Poss, E M]]

[[Category: Hydrogen tunneling]]

[[Category: Lipoxygenase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5tr0 is ON HOLD  until Paper Publication
+==Lipoxygenase-1 (soybean) L754A mutant at 293K==
+<StructureSection load='5tr0' size='340' side='right' caption='[[5tr0]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
-Authors: Poss, E.M., Fraser, J.S.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5tr0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TR0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TR0 FirstGlance]. <br>
-Description: Lipoxygenase-1 (soybean) L754A mutant at 293K
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tqn|5tqn]], [[5tqp|5tqp]], [[5tqo|5tqo]]</td></tr>
-[[Category: Poss, E.M]]
+<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: Fraser, J.S]]
+<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=5tr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tr0 OCA], [http://pdbe.org/5tr0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tr0 RCSB], [http://www.ebi.ac.uk/pdbsum/5tr0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tr0 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]]