Results - Active sites

Comparison of seven active sites (the term is defined in the methodology) showed similarity in polarity electrically charged amino acids and their spatial arrangement.


Fig. 6



In CYP1A2 are two negatively charged residues in helix I, tethered their functional groups are oriented toward the heme. Cofactor CYP2A6 has only one residue, which is reversed solvation channel. (Fig. 6)



Fig. 7





Active sites of cytochromes 2C8 and 2C9 are sequentially and functionally identical

(Fig. 7). Their amino acid 293 ASP  is an analogy ASP 313 (CYP1A2).
Cytochrome 2D6 contains other analogous residue occurring in the helix K and I. The ASP 368 - ASP 360 and ASP 301 - ASP 293.

 

Fig. 8



The last structures are enzymes 3A4 subfamilies. The polar residues from both structures agree. Here we can clearly see the work ARG 212, which become an antagonist of GLU 308 due to deliver of helix movement. GLU 308, in both cases, is similar as ASP 320 (in CYP1A2) and Glu 304 (in CYP2A6) (Fig. 8).