EC Number   |
|---|
    1.14.14.1 | 3D modeling of CYP51, presence of characteristic P450 motifs with a exceptionally large reductase interaction site 2. A number of mutations can be associated with ketoconazole resistance, especially at the channel entrance to the active site. Better stabilization of itraconazole, compared to ketoconazole, maybe due to a hydrogen bond with residue Asn230 |
| 1.14.14.1 | crystal structure of the complex between the heme- and FMN-binding domains of the enzyme, crystals are grown at room temperature by liquid-liquid free interface diffusion in a capillary, the flavodoxin-like flavin domain is positioned at the proximal face of the heme domain |
| 1.14.14.1 | crystallization of the wild-type and mutant CYP102A1 with and without bound substrates and one including theFMNbinding domain |
| 1.14.14.1 | homology model based on bacterial CYP102 and insect CYP6B4 |
| 1.14.14.1 | molecular dynamics simulations on two CYP102A1 mutants in complex with (-)-alpha-pinene to explore the molecular mechanism of substrate recognition and to predict regioselectivity. |
| 1.14.14.1 | purified recombinant mutant enzyme H226Y in complex with bifonazole, X-ray diffraction structure determination and analysis at 2.3 A resolution |
| 1.14.14.1 | structure of full-length CYP116B46. The continuous polypeptide chain comprises three functional domains, which align with the direction of electrons traveling from FMN to the heme through the [2Fe-2S] cluster. FMN and the [2Fe-2S] cluster are positioned closely, which facilitates efficient electron shuttling. The edge-to-edge straight-line distance between the [2Fe-2S] cluster and heme is approx. 25.3 A |
