In this study, organometallic compounds for RNase A protein inhibition are identified. It was essential for the present study to select organometallic complexes having potential biological activity and for this purpose 28 organometallic complexes were chosen for the study. Four compounds with a general structure (η6-p-Cymene)-((E)-9-nitro-6-(α-picolylimino)-7,12-dihydroindolo(3,2-d)(1)benzazepine-N,N')-chloro-metal(ii) chloride (2, 5-7) showed high protein binding properties in docking studies. This study revealed that complexes with Ruthenium and Osmium as metal centers were outperforming. Compound 2displayed the best results among them. Interestingly among compound 2 and 7 which are diastereomers, only one isomer is preferred for the binding process. From Hirshfeld surface analysis studies of the compounds, it was revealed that in comparison to compounds 5-7, compound 2 have far better amphiphilic nature which paved way for its hydrogen bond formation and different π-staking interactions with the amino acid of the protein. Its soft nature and its potential for RNase A inhibition can be linked to the higher energy of HOMO and lower energy of LUMO.