For membrane-associated enzymes, which access substrate from either a monolayer or bilayer of the aggregate substrate, the partitioning from the aqueous phase to this phospholipid interface is critical for catalysis. Despite a large and expanding body of knowledge regarding interfacial enzymes, the biophysical steps involved in interfacial recognition and adsorption remain relatively poorly understood. The surface of the enzyme that contacts the phospholipid surface is referred to as its interfacial binding surface, or more simply, its i-face. The interaction of a protein's i-face with the aggregate substrate may simply control access to substrate. However, it can be more complex, and this interaction often serves to allosterically activate the enzyme on this surface. First we briefly review what is currently known about i-face structure and function for a prototypical interfacial enzyme, the secreted Phospholipase A2 (PLA2). Then we develop, characterize, compare, and discuss models of the PLA2 i-face across a subset of five homologous PLA2 family members, groups IA, IB, IIA, V, and X. A homology model of human group-V is included in this comparison, suggesting that a similar approach could be used to explore interfacial function of any of the PLA2 family members. Despite moderate sequence identity, structural homology and sequence similarity are well conserved. We find that the residues predicted to be interfacial, while conserved structurally, are not highly conserved in sequence. Implications for this divergence on interfacial selectivity are discussed.