3sza

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Current revision (13:12, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3sza' size='340' side='right'caption='[[3sza]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
<StructureSection load='3sza' size='340' side='right'caption='[[3sza]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3sza]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SZA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3sza]] 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=3SZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SZA FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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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]] 1.48&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3sz9|3sz9]], [[3szb|3szb]]</div></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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALDH3, ALDH3A1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(P)(+)) Aldehyde dehydrogenase (NAD(P)(+))], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.5 1.2.1.5] </span></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=3sza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sza OCA], [https://pdbe.org/3sza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sza RCSB], [https://www.ebi.ac.uk/pdbsum/3sza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sza ProSAT]</span></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=3sza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sza OCA], [https://pdbe.org/3sza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sza RCSB], [https://www.ebi.ac.uk/pdbsum/3sza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sza ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/AL3A1_HUMAN AL3A1_HUMAN]] ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.
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[https://www.uniprot.org/uniprot/AL3A1_HUMAN AL3A1_HUMAN] ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human aldehyde dehydrogenases (ALDH) comprise a family of seventeen homologous enzymes that metabolize different biogenic and exogenic aldehydes. To date, there are relatively few general ALDH inhibitors that can be used to probe the contribution of this class of enzymes to particular metabolic pathways. Here, we report the discovery of a general class of ALDH inhibitors with a common mechanism of action. The combined data from kinetic studies, mass spectrometric measurements and crystallographic analyses demonstrate that these novel inhibitors undergo an enzyme-mediated beta-elimination reaction generating a vinyl-ketone intermediate that covalently modifies the active site cysteine residue present in these enzymes. The studies described here can provide the basis for rational approach to design ALDH isoenzyme-specific inhibitors as research tools and perhaps as drugs, to address diseases, such as cancer, where increased ALDH activity is associated with cellular phenotype.
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Discovery of a novel class of covalent inhibitor for aldehyde dehydrogenases.,Khanna M, Chen CH, Kimble-Hill A, Parajuli B, Perez-Miller S, Baskaran S, Kim J, Dria K, Vasiliou V, Mochly-Rosen D, Hurley TD J Biol Chem. 2011 Oct 21. PMID:22021038<ref>PMID:22021038</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3sza" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]]
*[[Aldehyde dehydrogenase 3D structures|Aldehyde dehydrogenase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hurley, T D]]
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[[Category: Hurley TD]]
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[[Category: Khanna, M]]
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[[Category: Khanna M]]
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[[Category: Aldh]]
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[[Category: Oxidoreductase]]
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[[Category: Rossmann fold]]
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Current revision

Crystal structure of human ALDH3A1 - apo form

PDB ID 3sza

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