Fig. 4: Structural diversification of clade 2 FUTs.
From: Structure, function, and implications of fucosyltransferases in health and disease
a Secondary-structure conservation heat map for clade 2 FUTs, mapped onto the FUT9 reference structure, with an inset showing conserved contacts at the GDP-Fuc binding pocket. b PROMALS3D alignment of the C-terminal catalytic domains from human FUT3, FUT4, FUT5, FUT6, FUT7, FUT9, POFUT3 and POFUT4 (UniProt IDs P21217, P22083, Q11128, P51993, Q11130, Q9Y231, Q6P4F1 and Q495W5, respectively). Annotation of secondary-structure elements, consensus positions, and residue coloring follows the same PROMALS3D scheme described in Fig. 3. The region of high conservation across all clade 2 FUTs are specifically highlighted in yellow. Heat maps integrate experimental crystal structures when available and rely on predictive models otherwise. GDP-Fuc is rendered opaque when positioned from crystallographic data and semi-transparent when model-derived. Methodological details regarding the integration of experimental structures with predictive models, the rendering of GDP-Fuc, and the use of transparency for side chains are described in Fig. 3.
