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[[Image:1lde.gif|left|200px]]<br />
<applet load="1lde" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1lde, resolution 2.5&Aring;" />
'''HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND N-FORMYL PIPERDINE'''<br />


==Overview==
==HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND N-FORMYL PIPERDINE==
Amides are analogs of aldehydes and potent inhibitors of liver alcohol, dehydrogenases. They can be used for structural studies and for inhibiting, the metabolism of alcohols that form toxic products. We studied N-alkyl, amides that bind to the enzyme-NADH complex and act as uncompetitive, inhibitors against varied concentrations of ethanol (millimolar Kii, values, at pH 8 and 25 degrees C): N-propylacetamide (16), delta-valerolactam (1.6), N-formylpiperidine (0.14), N-isobutylformamide, (0.028), N-(cyclohexylmethyl)-formamide (0.011), and N-cyclohexylformamide, (0.0087). The lower affinity of delta-valerolactam and N-propylacetamide, can be explained by steric hindrance with Phe93 of the enzyme. Replacing, Phe93 with Ala in the S48T/F93A mutated enzyme, which resembles the, natural ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9132002 (full description)]]
<StructureSection load='1lde' size='340' side='right'caption='[[1lde]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lde]] is a 4 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=1LDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LDE 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FPI:N-FORMYLPIPERIDINE'>FPI</scene>, <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=1lde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lde OCA], [https://pdbe.org/1lde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lde RCSB], [https://www.ebi.ac.uk/pdbsum/1lde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lde 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/ld/1lde_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=1lde ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1LDE 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 and FPI 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]]. Structure known Active Site: NAD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LDE OCA]].
*[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Binding of formamides to liver alcohol dehydrogenase., Ramaswamy S, Scholze M, Plapp BV, Biochemistry. 1997 Mar 25;36(12):3522-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9132002 9132002]
[[Category: Alcohol dehydrogenase]]
[[Category: Equus caballus]]
[[Category: Equus caballus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Plapp, B.V.]]
[[Category: Plapp BV]]
[[Category: Ramaswamy, S.]]
[[Category: Ramaswamy S]]
[[Category: FPI]]
[[Category: NAD]]
[[Category: ZN]]
[[Category: alcohol]]
[[Category: dehydrogenase]]
[[Category: formamides]]
[[Category: nicotinamide coenzyme]]
[[Category: oxidoreductase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:46:32 2007''

Latest revision as of 10:32, 14 February 2024

HORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND N-FORMYL PIPERDINEHORSE LIVER ALCOHOL DEHYDROGENASE COMPLEXED TO NADH AND N-FORMYL PIPERDINE

Structural highlights

1lde is a 4 chain structure with sequence from Equus caballus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADH1E_HORSE

Evolutionary Conservation

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

See Also

1lde, resolution 2.50Å

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