Malaria remains a public health challenge. Since many control strategies have proven ineffective in eradicating this disease, new strategies are required, among which the design of a multivalent vaccine stands out. However, the effectiveness of this strategy has been hindered, among other reasons, by the genetic diversity observed in parasite antigens. In Plasmodium vivax, the Erythrocyte Binding Protein (EBP, also known as DBP2) is an alternate ligand to Duffy Binding Protein (DBP); given its structural resemblance to DBP, EBP is proposed as a promising candidate for inclusion in vaccine design. However, the extent of genetic diversity within the locus encoding this protein has not been comprehensively assessed. Consequently, this study aims to characterize the genetic diversity of the pvebp locus, which encodes the P. vivax EBP protein, as well as assessing the evolutionary mechanisms that modulate this diversity. Using 36 Colombian pvebp gene sequences from P. vivax clinical parasitic isolates and 186 sequences available in databases, different parameters of intrapopulation genetic variation were estimated, evaluating their distribution worldwide, as well as the evolutionary forces that could determine the observed pattern of genetic variation. It was found that the pvebp gene exhibits one of the lowest levels of genetic diversity compared to other vaccine-candidate antigens. Four major haplotypes were shared worldwide. Analysis of the protein's 3D structure and epitope prediction identified five regions with potential antigenic properties. The obtained results suggest that the EBP protein possesses ideal characteristics to be considered during the design of a multivalent effective antimalarial vaccine against P. vivax.