Phosphoinositides (PIPs), phosphorylated derivatives of phosphatidylinositol (PI), are essential regulatory lipids involved in various cellular processes, including signal transduction, membrane trafficking, and cytoskeletal remodeling. To gain insight into the protein-PIP5 recognition process, it is necessary to study the inositol ring orientation (with respect to the membrane) of PIPS with different phosphorylation states. In this study, 8 PIPs (3 PIP, 2 PIP2, and 3 PIP3) with different phosphorylation and protonation sites have been separately simulated in two mixed bilayers (one with 20% phosphatidylserine (PS) lipids and another with PS lipids switched to phosphatidylcholine (PC) lipids), which roughly correspond to yeast membranes. Uniformity of the bilayer properties including hydrophobic thickness, acyl chain order parameters, and heavy atom density profiles is observed in both PS-contained and PC-enriched membranes due to the same hydrophobic core composition. The relationship between the inositol ring orientation (tilt and rotation angles) and its solvent-accessible surface area indicates that the orientation is mainly determined by its solvation energy. Different PIPs exhibit a clear preference in the inositol ring rotation angle. Surprisingly, a larger proportion of PIPs inositol rings stay closer to the surface of PS-contained membranes compared to PC-enriched ones. Such a difference is rationalized with the formation of more hydrogen bonds between the PS/PI headgroups and the PIPs inositol rings in PS-contained membranes. This hydrogen bond network could be functionally important; thus, the present results can potentially add important and detailed features into the existing protein-PIPs recognition mechanism.