COX (Cyclooxygenase) is the protein that infuses the degradation of PG (prostaglandins) from its substrate, AA (arachidonic acid). The reactions involve 2 steps that area unit 1 st step oxidation reaction of AA to hydroperoxy endoperoxide PGG2, go after by 2 nd steps future reduction to hydroxyl endoperoxide PGH2. During this work, we tend to study the interaction of ninety-seven flavone derivatives against COX enzymes for anti-inflammatory activity discovery using molecular docking simulation. Docking simulation for every compound was continual molegro virtual docker (MVD) 2013.6.0 for windows was used to predict the degree of each COX binding pockets. Thus, these observations are inconsistent 14 compounds were designated per their best marking values and were designed their hydrogen bonds, electrostatic interactions, steric interactions. However, selective CO-II inhibitors, respectively, N-acetyl-D-glucosamine, protoporphyrin-IX containing Fe, 1-Phenylsulfonamide-3-trifluoromethyl-5-parabromophenyl-pyrazole. The remainder of the LIGs is categorized as non-selective inhibitors.