Figure 7

Analysis of the three-dimensional structure of AEXynM. (A) The three-dimensional structure of AEXynM predicted by MODELLER 9.9. Two invariant catalytic residues, Glu⁸⁹ and Glu¹⁸⁰, reside at the center of an active region. The amino acid residues (Cys⁵, Pro⁹, and His¹⁴) mainly responsible for the high thermostability of AEXynM are located in β-strands A1 and B1, respectively. (B) One disulfide bridge (Cys⁵-Cys³²) is illustrated in the locally magnified three-dimensional structure. (C) The residues (Pro⁹, Phe²¹, and Trp²²) represented with spheres compose a hydrophobic interaction cluster. The hydrogen bond between His¹⁴ and Phe¹⁷ is illustrated with a dashed line.