4l2o: Difference between revisions

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==Crystal structure of human ALDH3A1 with its selective inhibitor 1-(4-fluorophenyl)sulfonyl-2-methylbenzimidazole==
==Crystal structure of human ALDH3A1 with its selective inhibitor 1-(4-fluorophenyl)sulfonyl-2-methylbenzimidazole==
<StructureSection load='4l2o' size='340' side='right' caption='[[4l2o]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
<StructureSection load='4l2o' size='340' side='right' caption='[[4l2o]], [[Resolution|resolution]] 1.94&Aring;' scene=''>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALDH3, ALDH3A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALDH3, ALDH3A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(P)(+)) Aldehyde dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.5 1.2.1.5] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_dehydrogenase_(NAD(P)(+)) Aldehyde dehydrogenase (NAD(P)(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.5 1.2.1.5] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l2o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l2o RCSB], [http://www.ebi.ac.uk/pdbsum/4l2o PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l2o OCA], [http://pdbe.org/4l2o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4l2o RCSB], [http://www.ebi.ac.uk/pdbsum/4l2o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4l2o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[[http://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.  
==See Also==
*[[Aldehyde dehydrogenase|Aldehyde dehydrogenase]]
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__TOC__
</StructureSection>
</StructureSection>

Revision as of 06:15, 5 August 2016

Crystal structure of human ALDH3A1 with its selective inhibitor 1-(4-fluorophenyl)sulfonyl-2-methylbenzimidazoleCrystal structure of human ALDH3A1 with its selective inhibitor 1-(4-fluorophenyl)sulfonyl-2-methylbenzimidazole

Structural highlights

4l2o is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Gene:ALDH3, ALDH3A1 (HUMAN)
Activity:Aldehyde dehydrogenase (NAD(P)(+)), with EC number 1.2.1.5
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

See Also

4l2o, resolution 1.94Å

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