A model of the enzyme PLA2 with a phospholipid substrate bound in the active site was derived using molecular graphics and molecular mechanics modelling techniques, and its ability to account for competitive inhibition tested by modelling the analogous complex of the enzyme and a known inhibitor; the model was then applied to the study of the binding of a new inhibitor, 3-arachidonyl-4(O-phosphoethanolamino)-methyltetrahydrofuran-2-one and the absolute stereochemistry for active site binding of this inhibitor predicted to be (3S,4R).