1teh

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(New page: 200px<br /> <applet load="1teh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1teh, resolution 2.7&Aring;" /> '''STRUCTURE OF HUMAN L...)
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[[Image:1teh.gif|left|200px]]<br />
 
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<applet load="1teh" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1teh, resolution 2.7&Aring;" />
 
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'''STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)'''<br />
 
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==Overview==
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==STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)==
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The crystal structure of the human class III chi chi alcohol dehydrogenase, (ADH) in a binary complex with NAD+(gamma) was solved to 2.7 A resolution, by molecular replacement with human class I beta1 beta1 ADH. chi chi ADH, catalyzes the oxidation of long-chain alcohols such as omega-hydroxy fatty, acids as well as S-hydroxymethyl-glutathione, a spontaneous adduct between, formaldehyde and glutathione. There are two subunits per asymmetric unit, in the chi chi ADH structure. Both subunits display a semi-open, conformation of the catalytic domain. This conformation is half-way, between the open and closed conformations described for the horse EE ADH, enzyme. The semi-open conformation and key changes in elements of, secondary structure provide a structural basis for the ability of chi ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9018047 (full description)]]
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<StructureSection load='1teh' size='340' side='right'caption='[[1teh]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1teh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TEH 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]] 2.7&#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=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=1teh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1teh OCA], [https://pdbe.org/1teh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1teh RCSB], [https://www.ebi.ac.uk/pdbsum/1teh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1teh ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADHX_HUMAN ADHX_HUMAN] Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.
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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/te/1teh_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=1teh ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1TEH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]] with ZN and NAD as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TEH OCA]].
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structure of human chi chi alcohol dehydrogenase: a glutathione-dependent formaldehyde dehydrogenase., Yang ZN, Bosron WF, Hurley TD, J Mol Biol. 1997 Jan 24;265(3):330-43. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9018047 9018047]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hurley, T.D.]]
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[[Category: Hurley TD]]
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[[Category: Yang, Z.N.]]
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[[Category: Yang Z-N]]
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[[Category: NAD]]
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[[Category: ZN]]
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[[Category: nad+ dependent alcohol dehydrogenase glutathione dependent formaldehyde dehydrogenase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 20:26:59 2007''
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Current revision

STRUCTURE OF HUMAN LIVER CHICHI ALCOHOL DEHYDROGENASE (A GLUTATHIONE-DEPENDENT FORMALDEHYDE DEHYDROGENASE)

PDB ID 1teh

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