Results - electrical polarity of the most important channels

The attached diagrams, we can notice that the enzyme in its internal structure substantially hydrophobic, electrically charged residues occur sporadically and out of the shell is apparent gradation of polarity.
 I deliberately focused on the comparison of sequentially related CYP, which is easier to find subtle differences in the analogies. ie, CYP2C8 and 2C9, CYP3A4 (1TQN and 2J0D).

SOLVATATION CHANNEL



Fig. 9 CYP2C: identity of residues GLU 300, ARG 307, ASP 165. Reverse polarity ARG 206 (2C8) and Glu 206 (2C9). LYS 199 is deflected from solvation channel.





Fig. 10 CYP3A: Identity ASP 174, LYS 173, GLU 163, LYS 168 (1TQN) - ARG 162 (2J0D) and helix F LYS 208. Replacement GLU 205 and LYS 209. LYS 487 (2J0D) makes a distant edge of the channel.

 

Fig. 11 CYP 2A6: a common positively charged region, LYS 476, HIS 477 (or ARG 311) with CYP1A2: LYS 500, HIS 501, ARG 503 (Fig. 12). Some of the CYP2A6 residues correspond to residues of other cytochromes:
 ARG 203 ≈ LYS 208, LYS 209 (2J0D), ARG 206 (2C8); ARG 311 ≈ ARG 307 (2C).

Fig. 12 In addition to CYP1A2, appears in all cytochromes a negatively charged residue at the beginning of helix E: 2C8, 2C9 - ASP 165, 3A4 - ASP 174, 2A6 - ASP 163, 2D6 - ASP 169.