EC Number   |
Reference |
|---|
   1.14.19.69 | complex of ferric CYP158A2 with substrate analogue 2-hydroxy-1,4-naphthoquinone, 2.15 A resolution, and the flaviolin ferrous dioxygen-bound CYP158A2 complex, to 1.8 A resolution. In the ferrous dioxygen-bound flaviolin complex, the three water molecules in the ferric flaviolin complex still occupy the same positions and form hydrogen bonds to the distal dioxygen atom. A continuous hydrogen-bonded water network connecting the active site to the protein surface is proposed to participate in the proton-delivery cascade, leading to dioxygen bond scission |
687501 |
| 1.14.19.69 | free enzyme and in complex with flaviolin, diffration to 1.75 and 1.62 A resolution, respectively.Upon ligand binding, a major conformational change takes place that closes the entry into the active site, partly due to repositioning of the F and G helices. Presence of two molecules of flaviolin in the closed active site that form a quasi-planar three-molecule stack including the heme |
687498 |
| 1.14.19.69 | free isoform CYP158A1, in complex with imidazole and in complex with flaviolin. Comparison of structures with isoform CYP158A2. In isoform CYP158A1, only one flaviolin molecule is present close to the heme iron, and the second flaviolin molecule binds at the entrance of the putative substrate access channel on the protein distal surface 9 A away |
685184 |
| 1.14.19.69 | I87K mutant of isoform CYP158A2, hanging drop vapor diffusion method, using 0.1 M bis-Tris (pH 6.5), 1.2 M ammonium dihydrogen phosphate |
726807 |
| 1.14.19.69 | in complex with inhibitor 4-phenylimidazole, crystallization in presence of malonic acid. Diffraction to 1.5 A resolution. Presence of malonic acid affects binding behaviour and increases inhibitory potency up to 2fold. Two molecules of malonate are found above the single inhibitor molecule in the active site, linked between the BC loop and beta 1-4/beta6-1 strands via hydrogen bond interactions to stabilize the conformational changes of the BC loop and beta strands that take place upon inhibitor binding. 4-Phenylimidazole can launch an extensive hydrogen-bonding network in the region of the F/G helices which may stabilize the conformational changes |
685076 |
