Figure 2
From: The conserved Phe GH5 of importance for hemoglobin intersubunit contact is mutated in gadoid fish
Modeling of Phe122β1- > Leu replacement in Atlantic cod hemoglobin. Superimposition of the three-dimensional model structures of Phe122β (red) and Leu122β (blue) variants in A) deoxy- and B) oxy-states. Surface structure of the α1β1 dimer is displayed with the α- and β-chains highlighted in dark gray and light gray, respectively. The B, G helices of α-chain (yellow) and the G, H helices and GH corner of β-chain (orange) are shown in ribbon representation. The closest distances from 122β1 residue to the α-chain are shown in Å.