AbstractCD6‐ligand interactions have been implicated in the regulation of T‐cell adhesion and activation. CD6 is a member of the scavenger receptor family, whereas its human ligand (ALCAM) belongs to the immunoglobulin superfamily. The extracellular region of ALCAM includes five immunoglobulin‐like domains. As a fusion protein, the N‐terminal extracellular domain of ALCAM (ALCAMD1) binds specifically to CD6. We report the construction, assessment, and analysis of a molecular model of ALCAMD1. The model defines the CDR‐analogous loops, the location of N‐linked glycosylation sites, and residues that form the β‐sheet faces of the immunoglobulin‐like domain. Predicted structural characteristics of the A'GFCC “C” face of the model are consistent with the presence of monomeric and dimeric forms of ALCAMD1, which has implications for the receptor‐ligand interactions.