Crystal structure of human short-chain acyl CoA dehydrogenase

SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE,

SCAD, BUTYRYL-COA DEHYDROGENASE, ACYL COA DEHYDROGENASE

0.2M AMMONIUM CHLORIDE, 20% PEG6000, 10% ETHYLENE GLYCOL, 0.1M TRIS-HCL PH8.0

GLY209 -> SER CHANGE IS A NATURAL VARIANT

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DENSITY ADJACENT TO FAD IN THE ACTIVE SITE HAS BEEN MODELLED AS COENZYME-A PERSULPHIDE. BOUND COS IS MOST APPARENT IN CHAIN G BUT NOT FULLY OCCUPIED IN OTHER CHAINS. NO ATTEMPT WAS MADE TO MODEL OCCUPANCY SO TEMPERATURE FACTORS ARE HIGH.
SHORT-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, (E.C.1.3.99.2)
FATTY ACID METABOLISM, FAD, POLYMORPHISM, FLAVOPROTEIN, MITOCHONDRION, DISEASE MUTATION, LIPID METABOLISM, OXIDOREDUCTASE, BETA OXIDATION, TRANSIT PEPTIDE