Conformational fidelity and hydrogen bond associability of L-histidine with sulfamate anion studied through XRD, quantum chemical, spectroscopic and molecular docking simulation as a cdk-4 inhibitor against retinoblastoma

•The single crystal L-Histidinium sulfamate was prepared and 3D structure is reported.•Theoretical molecular geometry, FT-IR and electronic spectrum were analysed.•NBO analysis explained the stability of the compound through hyper conjugative interaction.•Hirshfeld shows the interaction between the atoms.•Molecular docking simulation reveals the inhibitory potential of L-histidinium sulfamate against Cdk-4 protein.