1ped: Difference between revisions

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[[Image:1ped.png|left|200px]]


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==BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)==
The line below this paragraph, containing "STRUCTURE_1ped", creates the "Structure Box" on the page.
<StructureSection load='1ped' size='340' side='right'caption='[[1ped]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1ped]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PED OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PED FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.15&#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=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_1ped|  PDB=1ped  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ped FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ped OCA], [https://pdbe.org/1ped PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ped RCSB], [https://www.ebi.ac.uk/pdbsum/1ped PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ped ProSAT]</span></td></tr>
 
</table>
===BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)===
== Function ==
 
[https://www.uniprot.org/uniprot/ADH_CLOBE ADH_CLOBE] 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 active with acetaldehyde and propionaldehyde.<ref>PMID:8349550</ref> <ref>PMID:20102159</ref>
 
== Evolutionary Conservation ==
<!--
[[Image:Consurf_key_small.gif|200px|right]]
The line below this paragraph, {{ABSTRACT_PUBMED_15299659}}, adds the Publication Abstract to the page
Check<jmol>
(as it appears on PubMed at http://www.pubmed.gov), where 15299659 is the PubMed ID number.
  <jmolCheckbox>
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    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pe/1ped_consurf.spt"</scriptWhenChecked>
{{ABSTRACT_PUBMED_15299659}}
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
[[1ped]] is a 4 chain structure of [[Alcohol dehydrogenase]] with sequence from [http://en.wikipedia.org/wiki/Clostridium_beijerinckii Clostridium beijerinckii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PED OCA].  
</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=1ped ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
*[[Alcohol dehydrogenase|Alcohol dehydrogenase]]
*[[Tetrameric alcohol dehydrogenases|Tetrameric alcohol dehydrogenases]]
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:015299659</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Clostridium beijerinckii]]
[[Category: Clostridium beijerinckii]]
[[Category: Frolow, F.]]
[[Category: Large Structures]]
[[Category: Korkhin, Y.]]
[[Category: Frolow F]]
[[Category: Nadp]]
[[Category: Korkhin Y]]
[[Category: Oxidoreductase]]
[[Category: Thermostable]]

Latest revision as of 08:54, 17 April 2024

BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)BACTERIAL SECONDARY ALCOHOL DEHYDROGENASE (APO-FORM)

Structural highlights

1ped is a 4 chain structure with sequence from Clostridium beijerinckii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.15Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADH_CLOBE 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 active with acetaldehyde and propionaldehyde.[1] [2]

Evolutionary Conservation

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

See Also

References

  1. ↑ Ismaiel AA, Zhu CX, Colby GD, Chen JS. Purification and characterization of a primary-secondary alcohol dehydrogenase from two strains of Clostridium beijerinckii. J Bacteriol. 1993 Aug;175(16):5097-105. PMID:8349550
  2. ↑ Goihberg E, Peretz M, Tel-Or S, Dym O, Shimon L, Frolow F, Burstein Y. Biochemical and Structural Properties of Chimeras Constructed by Exchange of Cofactor-Binding Domains in Alcohol Dehydrogenases from Thermophilic and Mesophilic Microorganisms. Biochemistry. 2010 Feb 9. PMID:20102159 doi:10.1021/bi901730x

1ped, resolution 2.15Å

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OCA
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