In CYP450s, it is well known that the heme propionate forms a well-organized chain connected through the H-bonds, therefore, we performed water population analysis (SI) and water-heme H-bond analysis around 5 Å of Heme for different water models for all three complexes. Interestingly, among all the water models, the TIP3P water model has the maximum water count for CYP450BM3 while the TIP3P water count observed to be less for the CYP450BSβ, and CYP450OleT. At the same time, the OPC water model exhibits greater number of water molecules in case of CYP450OleT and CYP450BSβ. We note that the hydrophobicity of the active site is higher in CYP450BM3 due to the Phe87 and substrate hydrophobic tail while, in contrast, the active site in CYP450OleT and CYP450BSβ are more polar due to charged end of the substrate and an Arg245/Arg242 residues. Therefore, it could be anticipated that due to the more accurate distribution of point charges in OPC which mimic the optimal electrostatics of water models and the hydrophilic nature of active sites (in CYP450OleT and CYP450BSβ) supports the electrostatic interactions like H-bonds. Moreover, for CYP450BM3 where the active site is hydrophobic in nature, higher water populations (SI) and the H-bonds were observed for TIP3P water model. Therefore, we may conclude that TIP3P and SPC/E could be more suitable models for the hydrophobic active site while the OPC water model is more suitable for the polar active sites. Dipole moment: In a recent study, we have shown that the local electric field of the CYP450 enzyme could dictate the specific functions, and the dipole moment induced by the enzymatic local electric field could significantly catalyze the reaction by lowering the activation energy. Therefore, it is intriguing to study how the different water models affect the electrostatics of the active site residues. For so doing, we selected the 11 snapshots each at the interval of 10 ns (0ns, 10ns, 20ns, 30ns, -----100ns) and calculated the dipole moment due to the water molecules present near the 5 Å of the active site heme fragment. Table represents the average dipole moment for each model for all three enzymes. As can be seen, the dipole moment due to the water molecules is higher in the case of TIP3P for CYP450BM3 only, while OPC shows higher dipole moment for both peroxygenases, i.e., CYP450OleT and CYP450BSβ. The rationale for these different dipole moments could again be correlated with the hydrophobicity and the polarity of the active sites in all three enzymes.