4LRT
Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site
Summary for 4LRT
| Entry DOI | 10.2210/pdb4lrt/pdb |
| Related | 4LRS |
| Descriptor | 4-hydroxy-2-oxovalerate aldolase, Acetaldehyde dehydrogenase, PYRUVIC ACID, ... (9 entities in total) |
| Functional Keywords | rosmmann fold, tim barrel, dehydrogenase, aldolase, lyase-oxidoreductase complex, lyase/oxidoreductase |
| Biological source | Thermomonospora curvata More |
| Total number of polymer chains | 4 |
| Total formula weight | 145229.53 |
| Authors | Fischer, B.,Branlant, G.,Talfournier, F.,Gruez, A. (deposition date: 2013-07-20, release date: 2013-09-04, Last modification date: 2024-11-06) |
| Primary citation | Fischer, B.,Branlant, G.,Talfournier, F.,Gruez, A. Crystal and solution structures of the bifunctional enzyme (Aldolase/Aldehyde dehydrogenase) from Thermomonospora curvata, reveal a cofactor-binding domain motion during NAD+ and CoA accommodation whithin the shared cofactor-binding site To be Published, |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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