In the science of immunology, antibodies occupy a pivotal role, since they are protein molecules directed against harmful antigens by recognizing foreign molecules or antigens. Antibodies being the essence of an immune response are heavily studied molecules whose Human Antibody Light Chain Variable Domains (HALCVD) were our interest of study. We represented antibody structures as residue interaction networks, and our goal was to determine how useful closeness centrality is in identifying the CDR regions’ residues. The study utilized a dataset comprising of 120 antibodies, both free and bound. Only 4% of the statistically significant central residues belonged to the CDR L1, CDR L2, and CDR L3 regions. While almost 60% of the statistically significant central residues fell in the Fr regions flanking the CDR regions. Moreover, a staggering 61% of the statistically significant peripheral residues were found to belong to the CDR regions. On the other hand, we saw that some of the residues flanking CDR L1 and CDR L3 are centrally conserved, even though they are not a part of the CDR regions. © RJPT All right reserved.