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. Author manuscript; available in PMC: 2020 Aug 1.
Published in final edited form as: Int J Biol Macromol. 2019 May 10;134:445–457. doi: 10.1016/j.ijbiomac.2019.05.060

Figure 5.

Figure 5

Representative lowest energy binding configuration for Mg(II)PPIX and HSA at the heme binding site. Panel (A) shows the interaction between the PP and several amino acid residues that contribute to the energy minimization. Aromatic amino acids (Tyr138, Tyr161 and Phe134) are in green, aliphatic amino acids (Leu115, Leu135 and Ile142) are in orange and cationic residues (Arg114, Arg186 and Lys190) are in blue. Panel (B) shows the porphyrin ring sandwiched between Tyr138 and Tyr161 (in green). Panel (C) shows the general location of the binding site within the HSA.