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New page: left|200px<br /><applet load="1hld" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hld, resolution 2.1Å" /> '''STRUCTURES OF HORSE L...
 
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[[Image:1hld.jpg|left|200px]]<br /><applet load="1hld" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hld, resolution 2.1&Aring;" />
'''STRUCTURES OF HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH NAD+ AND SUBSTITUTED BENZYL ALCOHOLS'''<br />


==Overview==
==STRUCTURES OF HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH NAD+ AND SUBSTITUTED BENZYL ALCOHOLS==
Structures of the enzyme complexed with NAD+ and, 2,3,4,5,6-pentafluorobenzyl alcohol were determined by X-ray, crystallography at a resolution of 2.1 A and to a refinement R value of, 18.3% for a monoclinic (P2(1)) form and to 2.4 A and an R value of 18.9%, for a triclinic crystal form. The pentafluorobenzyl alcohol does not, react, due to electron withdrawal by the fluorine atoms. A structure with, NAD+ and p-bromobenzyl alcohol in the monoclinic form was also determined, at 2.5 A and an R value of 16.7%. The conformations of the subunits in the, monoclinic and triclinic crystal forms are very similar. The dimer is the, asymmetric unit, and a rigid body rotation closes the cleft between the, coenzyme and catalytic domains upon complex formation. In the monoclinic, form, this conformational change is described by a rotation of 9 degrees, in one subunit and 10 degrees in the other. The pentafluoro- and, p-bromobenzyl alcohols bind in overlapping positions. The hydroxyl group, of each alcohol is ligated to the catalytic zinc and participates in an, extensive hydrogen-bonded network that includes the imidazole group of, His-51, which can act as a base and shuttle a proton to solvent. The, hydroxymethyl carbon of the pentafluorobenzyl alcohol is 3.4 A from C4 of, the nicotinamide ring, and the pro-R hydrogen is in a good position for, direct transfer to C4. The p-bromobenzyl alcohol may react after small, rotations around single bonds of the alcohol. These structures should, approximate the active Michaelis-Menten complexes.
<StructureSection load='1hld' size='340' side='right'caption='[[1hld]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hld]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HLD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BRB:PARA-BROMOBENZYL+ALCOHOL'>BRB</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PFB:2,3,4,5,6-PENTAFLUOROBENZYL+ALCOHOL'>PFB</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=1hld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hld OCA], [https://pdbe.org/1hld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hld RCSB], [https://www.ebi.ac.uk/pdbsum/1hld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hld ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ADH1E_HORSE ADH1E_HORSE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/1hld_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1hld ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1HLD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equus_caballus Equus caballus] with ZN, NAD, PFB and BRB 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=1HLD OCA].
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structures of horse liver alcohol dehydrogenase complexed with NAD+ and substituted benzyl alcohols., Ramaswamy S, Eklund H, Plapp BV, Biochemistry. 1994 May 3;33(17):5230-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8172897 8172897]
[[Category: Alcohol dehydrogenase]]
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Eklund, H.]]
[[Category: Eklund H]]
[[Category: Plapp, B.V.]]
[[Category: Plapp BV]]
[[Category: Ramaswamy, S.]]
[[Category: Ramaswamy S]]
[[Category: BRB]]
[[Category: NAD]]
[[Category: PFB]]
[[Category: ZN]]
[[Category: oxidoreductase(ch-oh(d)-nad(a))]]
 
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