Fig. 1

Structure analysis and activity measurement of xylanases S7-xyl and its mutants. a Molecular docking analysis was performed by AutoDock software in YASARA using hydrolyzed xylopentaose as ligand. The binding energy in the final docked structure was 9.49 kcal/mol. The nearest distance between ligand and the catalytic residues E159 and E265 are 2.2 Å and 3.5 Å, respectively. The overall structure of 2UWF is shown as gray surface. The ligand is shown as ball-and-stick model in yellow. Red sticks indicate the catalytic residues. The tunnel-like structures were calculated by CAVER and named as tun_1 (blue), tun_2 (green) and tun_3 (purple). b The relative activities of wild-type and the mutants. c Mapping the mutated residues on the structure of wild-type xylanase S7-xyl (2UWF) and the mutant 254RL1, respectively. Structures are shown as teal cartoon. The mutated residues are shown as pink surface