6TQM
Escherichia coli AdhE structure in its compact conformation
Summary for 6TQM
Entry DOI | 10.2210/pdb6tqm/pdb |
EMDB information | 10551 10552 10555 |
Descriptor | Aldehyde-alcohol dehydrogenase, FE (III) ION, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE (3 entities in total) |
Functional Keywords | bacterial metabolism, oxidoreductase |
Biological source | Escherichia coli K-12 |
Total number of polymer chains | 4 |
Total formula weight | 386419.04 |
Authors | Fronzes, R.,Pony, P. (deposition date: 2019-12-16, release date: 2020-06-03, Last modification date: 2023-11-15) |
Primary citation | Pony, P.,Rapisarda, C.,Terradot, L.,Marza, E.,Fronzes, R. Filamentation of the bacterial bi-functional alcohol/aldehyde dehydrogenase AdhE is essential for substrate channeling and enzymatic regulation. Nat Commun, 11:1426-1426, 2020 Cited by PubMed: 32188856DOI: 10.1038/s41467-020-15214-y PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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