The small outer capsid protein plays a stabilizing role in the viral assembly, adhering to the<br />capsid during the later stages of maturation. This protein acts as glue among adjacent<br />capsomers, protecting the virus against extreme changes. The small outer capsid protein of the<br />bacteriophage IME08 was modelled using structural protein homology. A trimeric protein<br />docking was developed with the best-scored model and important sites of the molecules<br />interfaces were identified. It was used the Swiss Model platform for developing the protein<br />structure. Reliability was assessed by the QMEAN, Verify3D and ERRAT indices. The quality of<br />the whole model was verified by Ramachandran plot and the trimerization model was<br />performed on the platform ClusPro 2.0 Protein-Protein Docking. The structure obtained has a<br />reliability estimator QMEANscore4 of 0.769, rating it as a suitable model. The Z-Score QMEAN<br />value was 0.133, showing that the obtained model is not different from the experimental<br />structures stored in PDB database. The estimators and the Ramachandran plot evaluated<br />positively the model. Finally we identified a loop between two secondary structures as an<br />important site of the interaction of small outer capsid proteins, indicating that from residues 35<br />to 41 are relevant in the trimerization process.