Figure 2 | Scientific Reports

Figure 2

From: Structure-based activity prediction of CYP21A2 stability variants: A survey of available gene variations

Figure 2

Structural analysis of novel point substitution in the human CYP21A2.

(A) Cartoon representation of the residues involved in the novel point mutations found. Residues are labeled and highlighted by orange spheres. Heme cofactor is depicted in sticks. Residues involved in POR interaction are depicted in blue. (B) and (C) Differences in electrostatic surface upon mutations. Electrostatic surfaces of the wild type L122 and R122 as well as of the R122 and H132 mutants are represented. Residues are indicated by arrows. Acidic regions are depicted in red and basic ones in blue. (D) Cartoon representation of the residue L107 in the structure. Residue L107 (in light blue sticks) points towards the heme’s propionate moiety at a distance of 4.31 Å. HEM: heme group. P: Progesterone. (E) Cartoon representation of the residue P335 in the structure. Residues located nearby in the 3D structure are also shown.

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