4lrs | pdb_00004lrs

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

spinqualitylabelsall models 4lrs, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4lrs is a 3 chain structure with sequence from Thermomonospora curvata and Thermomonospora curvata dsm 43183. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CL, FOR, GOL, MG, NAD, PEG, PYR, SO4 Related: 4lrt Gene: Tcur_0536 (Thermomonospora curvata DSM 43183), Tcur_0535 (Thermomonospora curvata DSM 43183) Activity: 4-hydroxy-2-oxovalerate aldolase, with EC number 4.1.3.39 Resources: FirstGlance, OCA, RCSB, PDBsum Function [D1A3K8_THECD] Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).[HAMAP-Rule:MF_01656] [D1A3K7_THECD] Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds (By similarity).[HAMAP-Rule:MF_01657] See Also Aldolase

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