EC Number   |
|---|
    1.1.1.184 | - |
| 1.1.1.184 | 5 mg/ml recombinant enzyme in 25 mM phosphate buffer, pH 8.0, with 10% glycerol, and 5 mM NADP+, hanging drop vapour diffusion method, against well solution containing 4.0-4.4 M sodium formate and 10% v/v glycerol, X-ray diffraction structure determination and analysis at 2.5 A resolution |
| 1.1.1.184 | apo-enzyme, diffraction to 2.7 A. Enzyme forms a homotetramer with broken 2-2-2 symmetry. In the apo-form, the entrance of the NADPH pocket is blocked by a surface loop |
| 1.1.1.184 | by the hanging-drop vapor diffusion method, to 2.7 A resolution, crystal form belongs to space group P212121 with cell dimensions of a=104.7 A, b=142.8 A, and c=151.8 A. It forms a homotetramer with a broken 2-2-2 symmetry. SCR contains an extended N-terminal peptide (i.e., residues 1-25) and a short helix (residues 26-30) projecting out from the core domain that may stabilize the oligomer. In the apo-SCR structure, the entrance of the NADPH pocket is blocked by a surface loop |
| 1.1.1.184 | C-terminal peroxisomal targeting sequence 1 of each subunit is involved in intersubunit interactions and buried in the interior of the tetrameric enzyme |
| 1.1.1.184 | computational docking experiments for four inhibitors. For flavonoid inhibitors, the flavonoid skeleton is the binding part of the molecule and sugar moieties are pointing outward, giving rise to a stabilizing effect |
| 1.1.1.184 | computational model of docking of 4¢-methoxyacetophenone to the Q245H mutant |
| 1.1.1.184 | crystallization to crystal forms I and II in the presence of NADPH. Form I crystals belong to the tetragonal space group P42, and diffract to 1.5 A resolution. Form II crystals belong to the tetragonal space group P41212, and diffract to 2.2 A resolution |
| 1.1.1.184 | homology modeling of native enzyme, enzyme lacking the extra loop domain, and exchange of the extra loop domain for the short extra loop of 3alpha/20beta-hydroxysteroid dehydrogenase |
| 1.1.1.184 | in complex with cofactor NADP+ and with NADP+ and substrate ethyl 2-oxo-4-phenylbutyrate, to 1.7 and 2.0 A resolution, respectively. Both crystals belong to space group P3121, with similar unit-cell parameters |
