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2nvb

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==Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases (ADHs)==
==Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases (ADHs)==
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<StructureSection load='2nvb' size='340' side='right' caption='[[2nvb]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='2nvb' size='340' side='right'caption='[[2nvb]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2nvb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33075 Atcc 33075]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NVB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2nvb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoanaerobacter_brockii Thermoanaerobacter brockii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NVB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ykf|1ykf]]</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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">adh ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29323 ATCC 33075])</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=2nvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvb OCA], [https://pdbe.org/2nvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nvb RCSB], [https://www.ebi.ac.uk/pdbsum/2nvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nvb ProSAT], [https://www.topsan.org/Proteins/ISPC/2nvb TOPSAN]</span></td></tr>
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<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>
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<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=2nvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nvb OCA], [http://pdbe.org/2nvb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nvb RCSB], [http://www.ebi.ac.uk/pdbsum/2nvb PDBsum], [http://www.topsan.org/Proteins/ISPC/2nvb TOPSAN]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://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.
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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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
<jmolCheckbox>
<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nv/2nvb_consurf.spt"</scriptWhenChecked>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nv/2nvb_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>
</jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
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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=2nvb ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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==See Also==
==See Also==
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
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*[[Alcohol dehydrogenase from Entamoeba histolytica|Alcohol dehydrogenase from Entamoeba histolytica]]
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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*[[Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases|Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases]]
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*[[D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica|D275P mutant of alcohol dehydrogenase from protozoa Entamoeba histolytica]]
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*[[Tetrameric alcohol dehydrogenases|Tetrameric alcohol dehydrogenases]]
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 33075]]
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[[Category: Large Structures]]
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[[Category: Burstein, Y]]
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[[Category: Thermoanaerobacter brockii]]
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[[Category: Dym, O]]
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[[Category: Burstein Y]]
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[[Category: Frolow, F]]
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[[Category: Dym O]]
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[[Category: Goihberg, E]]
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[[Category: Frolow F]]
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[[Category: ISPC, Israel Structural Proteomics Center]]
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[[Category: Goihberg E]]
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[[Category: Peretz, M]]
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[[Category: Peretz M]]
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[[Category: Tel-Or, S]]
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[[Category: Tel-Or S]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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[[Category: Structural genomic]]
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Current revision

Contribution of Pro275 to the Thermostability of the Alcohol Dehydrogenases (ADHs)

PDB ID 2nvb

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