This dataset contains structural models of ReBphP with different mutations and conformations. The models were generated using a chimeric AI-based structure prediction approach combining Chai-1 and Boltz predictions, followed by QM/MM geometry optimization of the chromophore binding site. High-resolution crystal structures were incorporated as homology templates to accurately model the biliverdin binding pocket and PHY-tongue region. Internal and solvent-exposed water molecules were additionally modeled, including conserved active-site waters relevant to the proposed biliverdin photoisomerization mechanism. The resulting structures represent optimized stationary-state models of ReBPH and provide a structural framework for analyzing chromophore–protein interactions and hydrogen-bonding networks.