Figure 3. The interfaces of EaBglA tetramer.

(A) The interface α involves residues from the α-helices α11 and α13, while the interface γ connects loops from the catalytic face. (B) Two hydrophobic clusters (labeled residues) with a two-fold symmetry stabilize the interface α along with few hydrogen bonds (dotted lines) between interfacing polar residues (sticks). (C) The interface γ is essentially linked by hydrogen bonds (dotted lines) and electrostatic interactions (Lys⁴¹-Glu³⁰⁰), forming a semi-circle (light blue) that connects two active sites.