The paper is organized as follows: first, the excitation energy ladder of the FCP complex is reported using various quantum chemical methods based on the QM/MM-optimized structure as well as along a trajectory. Subsequently, we discuss the differences between the electronic ground and excited state densities that are determined to identify the electrostatic effects of the protein environment on the Q y absorption of individual Chl molecules. Then, the electric field susceptibility of Chl-a and Chl-c pigments is reported. Finally, we present the linear absorption spectrum of the FCP complex and the contribution of the Chl-a and Chl-c molecules. At the end of the manuscript, the physiological consequences of the findings are discussed in relation to the experimental literature and especially regarding the potential implications on the exciton dynamics of the studied FCP complex.