And so this substrate will not bind onto that active site simply because there is no space to actually go into that active site. Now, the question that you might ask is, why is it that the red molecule, the inhibitor, binds into the active side and not the green molecule, the substrate? Well, because normally the affinity of that inhibitor for that active side is much higher than the affinity of that substrate. And that's exactly why if given the chance to, if we mix these three molecules, because this has a much higher affinity for the active side than the substrate, this will be much more likely to actually bind into that active side to form that enzyme inhibitor mixture, enzyme inhibitor complex. Now, the defining point about competitive inhibition that you should know is because that inhibitor binds into the active side the same region where the substrate actually binds to, we can actually kick off that inhibitor from the active side by increasing the concentration of the substrate. And that's because when we increase the number of the green substrate molecules, there is much higher mathematical probability chance that the substrate will essentially collide with the active side and go into that active side.