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)