3fpl: Difference between revisions

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 ==Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii ADH by T. brockii ADH==
-<StructureSection load='3fpl' size='340' side='right' caption='[[3fpl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='3fpl' size='340' side='right'caption='[[3fpl]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3fpl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"clostridium_rubrum"_ng_and_vaughn_1963 "clostridium rubrum" ng and vaughn 1963]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FPL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3fpl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii] and [https://en.wikipedia.org/wiki/Thermoanaerobacter_brockii Thermoanaerobacter brockii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FPL FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3fpc|3fpc]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ADH1, ADH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1520 "Clostridium rubrum" Ng and Vaughn 1963])</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=3fpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpl OCA], [https://pdbe.org/3fpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fpl RCSB], [https://www.ebi.ac.uk/pdbsum/3fpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fpl ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(NADP(+)) Alcohol dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.2 1.1.1.2] </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=3fpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fpl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fpl RCSB], [http://www.ebi.ac.uk/pdbsum/3fpl PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ADH_CLOBE ADH_CLOBE]] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is active with acetaldehyde and propionaldehyde.<ref>PMID:8349550</ref> <ref>PMID:20102159</ref>
+[https://www.uniprot.org/uniprot/ADH_THEBR ADH_THEBR] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.[https://www.uniprot.org/uniprot/ADH_CLOBE ADH_CLOBE] Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is active with acetaldehyde and propionaldehyde.<ref>PMID:8349550</ref> <ref>PMID:20102159</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/fp/3fpl_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fp/3fpl_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=3fpl ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3fpl" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
-*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii ADH by T. brockii ADH|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of C. beijerinckii ADH by T. brockii ADH]]
+*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
-*[[Chimeras of alcohol dehydrogenases|Chimeras of alcohol dehydrogenases]]
-*[[Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH|Q165E/S254K Double Mutant Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH]]
-*[[Tetrameric alcohol dehydrogenases|Tetrameric alcohol dehydrogenases]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Clostridium rubrum ng and vaughn 1963]]
+[[Category: Clostridium beijerinckii]]
-[[Category: Burstein, Y]]
+[[Category: Large Structures]]
-[[Category: Felix, F]]
+[[Category: Thermoanaerobacter brockii]]
-[[Category: Goihberg, E]]
+[[Category: Burstein Y]]
-[[Category: Shimon, L]]
+[[Category: Felix F]]
-[[Category: Bacterial alcohol dehydrogenase]]
+[[Category: Goihberg E]]
-[[Category: Chimera]]
+[[Category: Shimon L]]
-[[Category: Domain exchange]]
-[[Category: Metal-binding]]
-[[Category: Nadp]]
-[[Category: Oxidoreductase]]
-[[Category: Oxydoreductase]]