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. So by increasing the concentration of the green molecules we increase the likelihood that the green molecules will collide with the active site to form the enzyme substrate complex. And that's exactly why if we increase the concentration of the substrate those green molecules will eventually outcompete these red inhibitor molecules and that will bring back the velocity of that velocity or the rate of that enzyme back to its normal value. So once again, competitive inhibitors typically have a much higher thinly for the active side than natural substrate molecules.