2IMP
Crystal structure of lactaldehyde dehydrogenase from E. coli: the ternary complex with lactate (occupancy 0.5) and NADH. Crystals soaked with (L)-Lactate.
Summary for 2IMP
| Entry DOI | 10.2210/pdb2imp/pdb |
| Related | 2HG2 2ILU |
| Descriptor | Lactaldehyde dehydrogenase, SULFATE ION, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | protein-lactate-nadh ternary complex, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 53320.17 |
| Authors | Di Costanzo, L.,Gomez, G.A.,Christianson, D.W. (deposition date: 2006-10-04, release date: 2007-02-13, Last modification date: 2023-11-15) |
| Primary citation | Di Costanzo, L.,Gomez, G.A.,Christianson, D.W. Crystal Structure of Lactaldehyde Dehydrogenase from Escherichia coli and Inferences Regarding Substrate and Cofactor Specificity. J.Mol.Biol., 366:481-493, 2007 Cited by PubMed Abstract: Aldehyde dehydrogenases catalyze the oxidation of aldehyde substrates to the corresponding carboxylic acids. Lactaldehyde dehydrogenase from Escherichia coli (aldA gene product, P25553) is an NAD(+)-dependent enzyme implicated in the metabolism of l-fucose and l-rhamnose. During the heterologous expression and purification of taxadiene synthase from the Pacific yew, lactaldehyde dehydrogenase from E. coli was identified as a minor (PubMed: 17173928 DOI: 10.1016/j.jmb.2006.11.023 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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