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[[Image:1cdo.gif|left|200px]]


{{Structure
==ALCOHOL DEHYDROGENASE (E.C.1.1.1.1) (EE ISOZYME) COMPLEXED WITH NICOTINAMIDE ADENINE DINUCLEOTIDE (NAD), AND ZINC==
|PDB= 1cdo |SIZE=350|CAPTION= <scene name='initialview01'>1cdo</scene>, resolution 2.05&Aring;
<StructureSection load='1cdo' size='340' side='right'caption='[[1cdo]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
<table><tr><td colspan='2'>[[1cdo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gadus_morhua_callarias Gadus morhua callarias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CDO FirstGlance]. <br>
|ACTIVITY= [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]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</td></tr>
|GENE=  
<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>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cdo OCA], [https://pdbe.org/1cdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cdo RCSB], [https://www.ebi.ac.uk/pdbsum/1cdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cdo ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ADH1_GADMC ADH1_GADMC]
== 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/cd/1cdo_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=1cdo ConSurf].
<div style="clear:both"></div>


'''ALCOHOL DEHYDROGENASE (E.C.1.1.1.1) (EE ISOZYME) COMPLEXED WITH NICOTINAMIDE ADENINE DINUCLEOTIDE (NAD), AND ZINC'''
==See Also==
 
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
The structural framework of cod liver alcohol dehydrogenase is similar to that of horse and human alcohol dehydrogenases. In contrast, the substrate pocket differs significantly, and main differences are located in three loops. Nevertheless, the substrate pocket is hydrophobic like that of the mammalian class I enzymes and has a similar topography in spite of many main-chain and side-chain differences. The structural framework of alcohol dehydrogenase is also present in a number of related enzymes like glucose dehydrogenase and quinone oxidoreductase. These enzymes have completely different substrate specificity, but also for these enzymes, the corresponding loops of the substrate pocket have significantly different structures. The domains of the two subunits in the crystals of the cod enzyme further differ by a rotation of the catalytic domains by about 6 degrees. In one subunit, they close around the coenzyme similarly as in coenzyme complexes of the horse enzyme, but form a more open cleft in the other subunit, similar to the situation in coenzyme-free structures of the horse enzyme. The proton relay system differs from the mammalian class I alcohol dehydrogenases. His 51, which has been implicated in mammalian enzymes to be important for proton transfer from the buried active site to the surface is not present in the cod enzyme. A tyrosine in the corresponding position is turned into the substrate pocket and a water molecule occupies the same position in space as the His side chain, forming a shorter proton relay system.
[[Category: Gadus morhua callarias]]
 
[[Category: Large Structures]]
==About this Structure==
[[Category: Eklund H]]
1CDO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gadus_callarias Gadus callarias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDO OCA].
 
==Reference==
Crystal structure of cod liver class I alcohol dehydrogenase: substrate pocket and structurally variable segments., Ramaswamy S, el Ahmad M, Danielsson O, Jornvall H, Eklund H, Protein Sci. 1996 Apr;5(4):663-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8845755 8845755]
[[Category: Alcohol dehydrogenase]]
[[Category: Gadus callarias]]
[[Category: Single protein]]
[[Category: Eklund, Ramaswamy S.H.]]
[[Category: NAD]]
[[Category: ZN]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:23:02 2008''

Latest revision as of 09:42, 7 February 2024

ALCOHOL DEHYDROGENASE (E.C.1.1.1.1) (EE ISOZYME) COMPLEXED WITH NICOTINAMIDE ADENINE DINUCLEOTIDE (NAD), AND ZINCALCOHOL DEHYDROGENASE (E.C.1.1.1.1) (EE ISOZYME) COMPLEXED WITH NICOTINAMIDE ADENINE DINUCLEOTIDE (NAD), AND ZINC

Structural highlights

1cdo is a 2 chain structure with sequence from Gadus morhua callarias. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.05Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADH1_GADMC

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1cdo, resolution 2.05Å

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