2cf5: Difference between revisions

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-==CRYSTAL STRUCTURES OF THE ARABIDOPSIS CINNAMYL ALCOHOL DEHYDROGENASES, ATCAD5==
-<StructureSection load='2cf5' size='340' side='right' caption='[[2cf5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+==Crystal Structures of the Arabidopsis Cinnamyl Alcohol Dehydrogenases, AtCAD5==
+<StructureSection load='2cf5' size='340' side='right'caption='[[2cf5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2cf5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CF5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2cf5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CF5 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><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]] 2&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2cf6|2cf6]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cinnamyl-alcohol_dehydrogenase Cinnamyl-alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.195 1.1.1.195] </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=2cf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cf5 OCA], [https://pdbe.org/2cf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cf5 RCSB], [https://www.ebi.ac.uk/pdbsum/2cf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cf5 ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cf5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2cf5 RCSB], [http://www.ebi.ac.uk/pdbsum/2cf5 PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
+[https://www.uniprot.org/uniprot/CADH5_ARATH CADH5_ARATH] Involved in lignin biosynthesis in the floral stem. Catalyzes the final step specific for the production of lignin monomers. Catalyzes the NADPH-dependent reduction of coniferaldehyde, 5-hydroxyconiferaldehyde, sinapaldehyde, 4-coumaraldehyde and caffeyl aldehyde to their respective alcohols.<ref>PMID:12805615</ref> <ref>PMID:14745009</ref> <ref>PMID:15937231</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cf5_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/2cf5_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2cf5 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2cf5" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Acetylcholinesterase|Acetylcholinesterase]]
+*[[Acetylcholinesterase 3D structures|Acetylcholinesterase 3D structures]]
-*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
+*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 38: @@
 </StructureSection>
 [[Category: Arabidopsis thaliana]]
-[[Category: Cinnamyl-alcohol dehydrogenase]]
+[[Category: Large Structures]]
-[[Category: Camacho, R.]]
+[[Category: Camacho R]]
-[[Category: Davin, L B.]]
+[[Category: Davin LB]]
-[[Category: Kang, C.]]
+[[Category: Kang C]]
-[[Category: Lee, C.]]
+[[Category: Lee C]]
-[[Category: Lewis, N G.]]
+[[Category: Lewis NG]]
-[[Category: Moinuddin, S.]]
+[[Category: Moinuddin S]]
-[[Category: Youn, B.]]
+[[Category: Youn B]]
-[[Category: Lignin biosynthesis]]
-[[Category: Metal-binding]]
-[[Category: Nadp]]
-[[Category: Oxidoreductase]]