Abstract CCR5 antagonism, PD-L1 modulation, and broadly neutralizing antibodies (bN- Abs) represent complementary axes in immune modulation and viral control. To eval- uate whether these axes could physically co-assemble as a structural triplet, curated Protein Data Bank (PDB) structures for CCR5 (4MBS), PD-L1 (8GAD), and a PD- L1-targeted nanobody (5DXW) were analyzed using UCSF ChimeraX (daily build, 2025-10-13, macOS). Manual alignment and visual inspection identified no sterically permissible three-body geometry, suggesting that a direct CCR5–PD-L1–bNAb com- plex is structurally improbable. These observations support the interpretation that synergy across these axes occurs indirectly through regulatory and signaling interac- tions rather than physical co-binding. Full report and figures are included in the attached PDF.