A comprehension of the structure-elements relationship is basic for seeing how a protein functions. Earlier examination has indicated that the movement of a protein relates with intra-space elements happening at picosecond to millisecond timescales. In any case, the relationship's between space elements and the capacity of a protein is inadequately comprehended. Here we show that interchanges between the synergist and hemopexin spaces of lattice metalloprotease-1 (MMP1) on type-1 collagen fibrils relate with its action. Utilizing single-particle FRET (smFRET), we recognized practically important open adaptations where the two MMP1 areas are very much isolated, which were fundamentally missing for chemically latent point freak (E219Q) of MMP1 and could be regulated by an inhibitor or an enhancer of action.