So we have the enzyme, this is the active side, this is our allosteric site to which the red inhibitor can actually bind to. So once we have this enzyme, if we have the substrate in close proximity, and this is far away, the substrate will bind until the active side to basically form this particular enzyme substrate mixture and then the enzyme substrate complex. If no inhibitors bound onto that allosteric side, this can basically catalyze the transformation of that substrate, the green molecule, into the product and by the way, forgot to throw a product. So let's say that that green structure is transformed into this final molecule, which is our product, and this will only take place if no inhibitors actually bound onto that allosteric site. Now, instead, we can also have this pathway that is followed. If this is in close proximity, it binds onto the allosteric site to form that enzyme inhibitor complex.