A single predicted monomer structure is insufficient. It may suggest a possible binding pocket, domain hinge or subunit interface, and a confident multimer model may support a particular assembly hypothesis. Those features do not establish that alternative conformations are populated, that ligand binding shifts their populations, or that occupancy at one site changes another site's binding strength.
Cooperative allostery concerns free-energy relationships among states, not only one static geometry. Structural comparisons across conditions, independent oligomeric-mass measurements and ligand-dependent binding or activity curves are needed to test the proposal. A low-confidence inter-domain orientation is likewise uncertainty about a model, not a prediction that the protein is necessarily an allosteric oligomer.
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