1y9a
From Proteopedia
(Difference between revisions)
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<StructureSection load='1y9a' size='340' side='right'caption='[[1y9a]], [[Resolution|resolution]] 1.81Å' scene=''> | <StructureSection load='1y9a' size='340' side='right'caption='[[1y9a]], [[Resolution|resolution]] 1.81Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1y9a]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1y9a]] is a 2 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=1Y9A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y9A FirstGlance]. <br> |
- | </td></tr><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=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.81Å</td></tr> |
- | + | <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=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=OHS:O-(CARBOXYSULFANYL)-4-OXO-L-HOMOSERINE'>OHS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1y9a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y9a OCA], [https://pdbe.org/1y9a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y9a RCSB], [https://www.ebi.ac.uk/pdbsum/1y9a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y9a ProSAT]</span></td></tr> | |
- | + | ||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [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]] | ||
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*[[Alcohol dehydrogenase|Alcohol dehydrogenase]] | *[[Alcohol dehydrogenase|Alcohol dehydrogenase]] | ||
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] | *[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] | ||
- | *[[Alcohol dehydrogenase from Entamoeba histolytica|Alcohol dehydrogenase from Entamoeba histolytica]] | ||
- | *[[Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH|Chimera of alcohol dehydrogenase by exchange of the cofactor binding domain res 153-294 of T. brockii ADH by E. histolytica ADH]] | ||
- | *[[Chimeras of alcohol dehydrogenases|Chimeras of alcohol dehydrogenases]] | ||
- | *[[D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica|D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica]] | ||
- | *[[Tetrameric alcohol dehydrogenases|Tetrameric alcohol dehydrogenases]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Entamoeba histolytica]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Burstein | + | [[Category: Burstein Y]] |
- | [[Category: Frolow | + | [[Category: Frolow F]] |
- | [[Category: Goihberg | + | [[Category: Goihberg E]] |
- | [[Category: Peretz | + | [[Category: Peretz M]] |
- | [[Category: Shimon | + | [[Category: Shimon LJ]] |
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Revision as of 08:01, 15 May 2024
Alcohol Dehydrogenase from Entamoeba histolotica in complex with cacodylate
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