3hud

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(New page: 200px<br /> <applet load="3hud" size="450" color="white" frame="true" align="right" spinBox="true" caption="3hud, resolution 3.2&Aring;" /> '''THE STRUCTURE OF HUM...)
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[[Image:3hud.gif|left|200px]]<br />
 
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<applet load="3hud" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="3hud, resolution 3.2&Aring;" />
 
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'''THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS'''<br />
 
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==Overview==
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==THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS==
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The three-dimensional structure of human beta 1 beta 1 alcohol, dehydrogenase (ADH; EC 1.1.1.1) complexed with NAD+ has been determined by, x-ray crystallography to 3.0-A resolution. The amino acids directly, involved in coenzyme binding are conserved between horse EE and human beta, 1 beta 1 alcohol dehydrogenase in all but one case [serine (horse) vs., threonine (human) at position 48]. As a result, the coenzyme molecule is, bound in a similar manner in the two enzymes. However, the strength of the, interactions in the vicinity of the pyrophosphate bridge of NAD+ appears, to be enhanced in the human enzyme. Side-chain movements of Arg-47 and, Asp-50 and a shift in the position of the helix comprising residues, 202-212 may explain both the decreased Vmax and the decreased rate of NADH, dissociation observed in the human enzyme vs. the horse enzyme. It appears, that these catalytic differences are not due to substitutions of any amino, acids directly involved in coenzyme binding but are the result of, structural rearrangements resulting from multiple sequence differences, between the two enzymes.
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<StructureSection load='3hud' size='340' side='right'caption='[[3hud]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3hud]] 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=3HUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HUD 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]] 3.2&#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=3hud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hud OCA], [https://pdbe.org/3hud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hud RCSB], [https://www.ebi.ac.uk/pdbsum/3hud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hud ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ADH1B_HUMAN ADH1B_HUMAN]
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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/hu/3hud_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=3hud ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known diseases associated with this structure: Alcoholism, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=103720 103720]]
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*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
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__TOC__
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==About this Structure==
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</StructureSection>
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3HUD 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]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=3HUD OCA].
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==Reference==
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Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions., Hurley TD, Bosron WF, Hamilton JA, Amzel LM, Proc Natl Acad Sci U S A. 1991 Sep 15;88(18):8149-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1896463 1896463]
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[[Category: Alcohol dehydrogenase]]
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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: Amzel, L.M.]]
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[[Category: Amzel LM]]
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[[Category: Bosron, W.F.]]
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[[Category: Bosron WF]]
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[[Category: Hamilton, J.A.]]
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[[Category: Hamilton JA]]
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[[Category: Hurley, T.D.]]
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[[Category: Hurley TD]]
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[[Category: NAD]]
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[[Category: ZN]]
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[[Category: oxidoreductase(nad(a)-choh(d))]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:48:57 2007''
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Current revision

THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS

PDB ID 3hud

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