Fig. 7
From: Purification and characterization of a novel cold adapted fungal glucoamylase
Structural comparison between glucoamylases from H. jecorina (HjGa) and Tetracladium sp. (AmyT1). a Superimposition of the predicted glucoamylase model of AmyT1 (green) and the structure of the glucoamylase from HjGa (blue). The linker region (red arrow) and variable loop (yellow arrow) are indicated. Residues involved in substrate recognition and in the catalytic site are shown in magenta and cyan, respectively, for AmyT1 (b) and HjGa (c). The calculated distances in Amy1T between residues Y47 and R309, W51 and Y315, W120 and Y315, and E190 and Y315 are 8.5, 9.6, 8.7 and 10.2 Å, respectively. For HjGa, the calculated distances between the equivalent residues Y47 and R309, W51 and Y315, W120 and Y315, and E190 and Y315 were 8.5, 8.6, 8.3 and 10.1 Å, respectively