Accordingly, and building on our previous computational investigations of the isolated MCR catalytic domain, we here sought to explore the conformational dynamics of the complete MCR protein using extended (500 ns) molecular dynamics simulations of an homology model in a model membrane environment, in order to investigate interactions with the phosphatidylethanolamine donor substrate and zinc cofactor in the ground (reactive) state, and the effect upon these of PEtN addition to Thr285 to form the covalent phosphointermediate. The results identify only limited motions of the two domains relative to one another and do not support stable binding of a second zinc equivalent under the conditions tested, while establishing that the complex of a donor substrate with the ground state enzyme is capable of sampling a stable and potentially reactive conformation.