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==D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica==
==D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica==
<StructureSection load='2oui' size='340' side='right' caption='[[2oui]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
<StructureSection load='2oui' size='340' side='right'caption='[[2oui]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2oui]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Enthi Enthi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OUI FirstGlance]. <br>
<table><tr><td colspan='2'>[[2oui]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OUI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OUI FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <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=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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]] 1.77&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1y9a|1y9a]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <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=NO3:NITRATE+ION'>NO3</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5759 ENTHI])</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=2oui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oui OCA], [https://pdbe.org/2oui PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oui RCSB], [https://www.ebi.ac.uk/pdbsum/2oui PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oui 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=2oui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oui OCA], [http://pdbe.org/2oui PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2oui RCSB], [http://www.ebi.ac.uk/pdbsum/2oui PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2oui ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ADH1_ENTHI ADH1_ENTHI]] 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.<ref>PMID:20102159</ref>
[https://www.uniprot.org/uniprot/ADH1_ENTHI ADH1_ENTHI] 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.<ref>PMID:20102159</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/2oui_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ou/2oui_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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==See Also==
==See Also==
*[[Alcohol dehydrogenase from Entamoeba histolytica|Alcohol dehydrogenase from Entamoeba histolytica]]
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
*[[D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica|D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica]]
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
*[[Tetrameric alcohol dehydrogenases|Tetrameric alcohol dehydrogenases]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Enthi]]
[[Category: Entamoeba histolytica]]
[[Category: Burstein, Y]]
[[Category: Large Structures]]
[[Category: Dym, O]]
[[Category: Burstein Y]]
[[Category: Frolow, F]]
[[Category: Dym O]]
[[Category: Goihberg, E]]
[[Category: Frolow F]]
[[Category: Peretz, M]]
[[Category: Goihberg E]]
[[Category: Shimon, L]]
[[Category: Peretz M]]
[[Category: Cacodylate ion]]
[[Category: Shimon L]]
[[Category: Metal-binding]]
[[Category: Nadp]]
[[Category: Oxidoreductase]]
[[Category: P275d mutation]]
[[Category: Tetramer]]
[[Category: Thermosatbility]]

Latest revision as of 08:58, 25 October 2023

D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica

2oui, resolution 1.77Å

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