4LRS
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 4LRS
Entry DOI | 10.2210/pdb4lrs/pdb |
Related | 4LRT |
Descriptor | 4-hydroxy-2-oxovalerate aldolase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, FORMYL GROUP, ... (12 entities in total) |
Functional Keywords | rossmann fold, tim barrel domain, dehydrogenase, aldolase, oxidoreductase |
Biological source | Thermomonospora curvata More |
Total number of polymer chains | 3 |
Total formula weight | 73954.12 |
Authors | Fischer, B.,Branlant, G.,Talfournier, F.,Gruez, A. (deposition date: 2013-07-20, release date: 2013-09-04, Last modification date: 2023-11-15) |
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 (1.55 Å) |
Structure validation
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