3ftn

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{{STRUCTURE_3ftn| PDB=3ftn | SCENE= }}
 
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===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===
 
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{{ABSTRACT_PUBMED_20102159}}
 
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==About this Structure==
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==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==
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[[3ftn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermoanaerobacter_brockii Thermoanaerobacter brockii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FTN OCA].
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<StructureSection load='3ftn' size='340' side='right'caption='[[3ftn]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3ftn]] is a 4 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=3FTN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FTN FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.192&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ftn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ftn OCA], [https://pdbe.org/3ftn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ftn RCSB], [https://www.ebi.ac.uk/pdbsum/3ftn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ftn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ft/3ftn_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3ftn ConSurf].
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<div style="clear:both"></div>
==See Also==
==See Also==
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
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*[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-295 of T. brockii ADH by C. beijerinckii ADH]]
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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*[[Chimeras of alcohol dehydrogenases|Chimeras of alcohol dehydrogenases]]
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== References ==
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*[[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]]
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<references/>
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*[[Tetrameric alcohol dehydrogenases|Tetrameric alcohol dehydrogenases]]
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Clostridium beijerinckii]]
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<ref group="xtra">PMID:020102159</ref><references group="xtra"/>
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[[Category: Large Structures]]
[[Category: Thermoanaerobacter brockii]]
[[Category: Thermoanaerobacter brockii]]
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[[Category: Burstein, Y.]]
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[[Category: Burstein Y]]
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[[Category: Frolow, F.]]
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[[Category: Frolow F]]
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[[Category: Goihberg, E.]]
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[[Category: Goihberg E]]
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[[Category: Shimon, L.]]
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[[Category: Shimon L]]
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[[Category: Bacterial alcohol dehydrogenase]]
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[[Category: Chimera]]
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[[Category: Domain exchange]]
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[[Category: Metal-binding]]
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[[Category: Nadp]]
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[[Category: Oxidoreductase]]
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[[Category: Oxydoreductase]]
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Current revision

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

PDB ID 3ftn

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