Alpha-L-fucosidases are essential tools for studying the structure-function relationships of fucosylated sugars and for the synthesis of glycoconjugates. Despite their significant potential in biotechnology, detailed structural and mechanistic aspects of these enzymes remain poorly understood. In this study, we identified a novel α-l-fucosidase from the fungus Fusarium proliferatum LE1, belonging to the GH29 family of glycoside hydrolases. The recombinant protein was purified and biochemically characterized. The crystal structure of the enzyme was determined at anisotropic resolution of 2.2-2.6 Å in the closed conformation of the active site. Structural comparison with homologous proteins revealed a conserved catalytic domain and a non-conserved C-terminal domain, which displays significant flexibility in the crystal, as confirmed by molecular dynamics simulations. We propose that this flexibility reflects intrinsic enzyme dynamics, enabling substrate recognition, binding, and translocation to the active site.