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. Author manuscript; available in PMC: 2022 Dec 15.
Published in final edited form as: Arch Biochem Biophys. 2021 Oct 31;714:109076. doi: 10.1016/j.abb.2021.109076

Fig. 8.

Fig. 8.

Model of P450 27C1-Adx interaction. Localization of P450 27C1 (A) and Adx (B) residues identified in cross-links. Residues are shown as sticks (red for Adx, blue for P450 27C1) and the rest of the structure is shown as cartoon (light orange for Adx, pale cyan for P450 27C1). (C–D) Modeled P450 27C1-Adx complexes ((C), cluster 4; (D), cluster 3). Residues identified from cross-linking data at the interface are shown as sticks, the rest of the structure is shown as a transparent surface. The heme of the P450 and the [2Fe-2S] cluster of Adx are shown in black. The distance between the [2Fe-2S] cluster and the center of the heme was 26.1 Å in the cluster 3 model and 44.8 Å in the cluster 4 model (shown as dashed line).