3dsi: Difference between revisions

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==Crystal Structure of Arabidopsis thaliana Allene Oxide Synthase (AOS, cytochrome P450 74A, CYP74A) Complexed with 13(S)-HOT at 1.60 A resolution==
==Crystal Structure of Arabidopsis thaliana Allene Oxide Synthase (AOS, cytochrome P450 74A, CYP74A) Complexed with 13(S)-HOT at 1.60 A resolution==
<StructureSection load='3dsi' size='340' side='right' caption='[[3dsi]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='3dsi' size='340' side='right'caption='[[3dsi]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3dsi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DSI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DSI FirstGlance]. <br>
<table><tr><td colspan='2'>[[3dsi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DSI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DSI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=T24:(9Z,11E,13S,15Z)-13-HYDROXYOCTADECA-9,11,15-TRIENOIC+ACID'>T24</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=T24:(9Z,11E,13S,15Z)-13-HYDROXYOCTADECA-9,11,15-TRIENOIC+ACID'>T24</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3dsj|3dsj]], [[3dsk|3dsk]], [[3cli|3cli]], [[2rch|2rch]], [[2rcl|2rcl]], [[2rcm|2rcm]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dsj|3dsj]], [[3dsk|3dsk]], [[3cli|3cli]], [[2rch|2rch]], [[2rcl|2rcl]], [[2rcm|2rcm]]</div></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP74A, AOS, At5g42650, MJB21.2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CYP74A, AOS, At5g42650, MJB21.2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroperoxide_dehydratase Hydroperoxide dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.92 4.2.1.92] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hydroperoxide_dehydratase Hydroperoxide dehydratase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.92 4.2.1.92] </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=3dsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dsi OCA], [http://pdbe.org/3dsi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dsi RCSB], [http://www.ebi.ac.uk/pdbsum/3dsi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dsi ProSAT]</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=3dsi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dsi OCA], [https://pdbe.org/3dsi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dsi RCSB], [https://www.ebi.ac.uk/pdbsum/3dsi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dsi ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/3dsi_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ds/3dsi_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</div>
</div>
<div class="pdbe-citations 3dsi" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 3dsi" style="background-color:#fffaf0;"></div>
==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
== References ==
<references/>
<references/>
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[[Category: Arath]]
[[Category: Arath]]
[[Category: Hydroperoxide dehydratase]]
[[Category: Hydroperoxide dehydratase]]
[[Category: Large Structures]]
[[Category: Lee, D S]]
[[Category: Lee, D S]]
[[Category: Nioche, P]]
[[Category: Nioche, P]]

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