EC Number   |
|---|
    2.3.1.87 | hanging-drop vapor diffusion method, mixing of 0.001 ml of both protein and reservoir solution, equilibration against 0.15 ml of reservoir solution containing 0.17 M ammonium acetate, 25.5% PEG 4000, and 17% glycerol, and 0.1 M sodium citrate, pH 5.6, X-ray diffraction structure determination and analysis, molecular replacement, modeling |
| 2.3.1.87 | molecular modeling, docking of N-acetylserotonin and screening for potential ligands. N-[2-(5-hydroxy-1H-indol-3-yl)ethy1]-3-(4-hydroxyphenyl)-2-propenamide show least binding energy, i.e. -9.38 Kcal/mol |
| 2.3.1.87 | solution NMR studies. AANAT3 is well-folded in solution. The P-loop, which is responsible for cofactor binding, is flexible in the free-state, while a large region of the enzyme interconverts between two distinct conformations in the slow exchange regime |
| 2.3.1.87 | structure of apoenzyme and in complex with acetyl-CoA, to 2.21 and 1.65 A resolution, respectively. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel |
