Fig. 5
From: Discovery of novel alkaline-tolerant xylanases from fecal microbiota of dairy cows
The modeling structures and structure comparisons of CDW-xyl-8 and CDW-xyl-16. A The predicted cartoon structure of CDW-xyl-8 by AlphaFold2, and its catalytic residues are E382 and E521. B The cartoon structure of CjXyn10C (PDB ID: 1US3), a known GH10 family xylanase, and its catalytic residues are E385 and E497. C Superimposition of CDW-xyl-8 model and CjXyn10C, they both adopted a typical (β/α)8 barrel fold of GH10 family xylanase, and the catalytic sites overlapped well. D The predicted cartoon structure of CDW-xyl-16 by SWISS-MODEL, and its catalytic residues are E106 and E215. E The cartoon structure of XynCDBFV (PDB ID: 3WP4), a known GH11 family xylanase, and its catalytic residues are E109 and E202. F Superimposition of CDW-xyl-16 model and XynCDBFV, they both displayed a typical β-jelly-roll fold of GH10 family xylanase, and the catalytic sites overlapped well. The α-helixes are colored with red, β-sheets are colored with yellow, turns and loops are colored with green, and the C atoms of catalytic residues are colored with bule in CDW-xyl-8 and CDW-xyl-16. The α-helixes are colored with cyan, β-sheets are colored with magenta, turns and loops are colored with salmon, and the C atoms of catalytic residues are colored with orange in CjXyn10C and XynCDBFV