The objective of this study was to investigate the reliability of a fragmental approach to build a full-length model of the human ghrelin receptor (hGHS-R1a) in its open state. The soundness of the model was verified by docking the tetrapeptide Gly-Ser-Ser(n-octanoyl)-Phe-NH2, which represents the ghrelin active core, and a dataset of 35 peptidomimetic GH secretagogues taken from literature. Docking results confirm the relevance of two distinct subpockets: a polar cavity bearing the key residues involved in receptor activation and an aromatic/apolar subpocket, which plays a crucial role in determining the high constitutive activity of hGHS-R1a. The docking scores of both subpockets are in remarkable agreement with biological data, emphasizing that the model can be used to predict the activity of novel ligands. Moreover, the subpocket selectivity of peptidomimetic GHSs suggests a cooperative role of the aromatic/apolar subpocket. Taken globally, the results highlight the potential of the fragmental approach to build improved models for any GPCR.