The　SARS-CoV-2　variant　BA.2.86　(Omicron)　has　emerged　with　unique　mutations　that　may　increase　its　transmission　and　infectivity.　This　study　investigates　how　these　mutations　alter　the　interaction　network　and　dynamic　properties　of　the　Omicron　receptor-binding　domain　(RBD)　compared　to　the　wild-type　virus,　focusing　on　its　binding　affinity　to　the　human　ACE2　(hACE2)　receptor.　Protein-protein　docking　and　all-atom　molecular　dynamics　simulations　were　used　to　analyze　structural　and　dynamic　differences.　Despite　the　structural　similarity,　the　Omicron　variant　exhibits　a　distinct　interaction　network　with　new　residues　such　as　Lys353　and　Arg498　that　significantly　enhance　its　binding　capacity.　The　dynamic　analysis　reveals　increased　flexibility　in　the　RBD,　particularly　in　loop　regions　crucial　for　hACE2　interaction.　Mutations　significantly　alter　the　secondary　structure,　leading　to　greater　flexibility　and　conformational　adaptability　compared　to　the　wild　type.　Binding　free　energy　calculations　confirm　that　the　Omicron　RBD　has　a　higher　binding　affinity　(-　70.47　kcal/mol)　to　hACE2　than　the　wild-type　RBD　(-　61.38　kcal/mol).　These　results　suggest　that　the　altered　interaction　network　and　enhanced　dynamics　of　the　Omicron　variant　contribute　to　its　increased　infectivity,　providing　insights　for　the　development　of　targeted　therapeutics　and　vaccines.