6ahc
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activity== | |
| - | + | <StructureSection load='6ahc' size='340' side='right'caption='[[6ahc]], [[Resolution|resolution]] 3.45Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6ahc]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AHC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AHC FirstGlance]. <br> | |
| - | + | </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=6ahc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ahc OCA], [http://pdbe.org/6ahc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ahc RCSB], [http://www.ebi.ac.uk/pdbsum/6ahc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ahc ProSAT]</span></td></tr> | |
| - | [[Category: | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/ADHE_ECOLI ADHE_ECOLI]] This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction. | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Kim, G]] | [[Category: Kim, G]] | ||
| - | [[Category: Song, J | + | [[Category: Song, J J]] |
| + | [[Category: Acetyl coa]] | ||
| + | [[Category: Ethanol]] | ||
| + | [[Category: High-order structure]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Regulation]] | ||
Revision as of 05:49, 21 August 2019
Cryo-EM structure of aldehyde-alcohol dehydrogenase reveals a high-order helical architecture critical for its activity
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