And so that inhibitor is just as likely to get into that active side as our substrate. So for this particular case, because we're assuming the affinity of this enzyme to the inhibitor is the same as to our substrate. So we see that once the inhibitor binds to the active side, this substrate cannot get inside, and so the enzyme is rendered inactive. Now, the special thing about competitive inhibition is the following. For a given fixed concentration of inhibitor, if we begin to increase the concentration of that substrate, for example, we create a four to one ratio of green to purple molecules. Now, what happens is these green substrate molecules are much more likely to actually bind into that active side than compared to our purple inhibitor molecule.