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Enzyme-Substrate Complex: 2'-Fucosyllactose and UDP-Gal Binding in Fucosyltransferase #1404195 (License: Personal Use)
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This high-resolution structural model depicts the binding of 2'-fucosyllactose and UDP-Gal to a human fucosyltransferase enzyme, revealing precise atomic interactions that drive human milk oligosaccharide (HMO) synthesis. Key catalytic residues-including W218, H122, N95, and D191-form hydrogen bonds and hydrophobic contacts with substrates, stabilizing the transition state. The image highlights the enzyme’s specificity for α-1,2-fucosylation, crucial for prebiotic and immunomodulatory functions in infant nutrition.
Used in academic publications, biotech product documentation, and educational resources on glycobiology or infant nutrition; targets researchers, students, and industry professionals seeking mechanistic insight into HMO biosynthesis enzymes.
Related Cliparts: Detailed 3D structure of a fucosyltransferase enzyme bound to 2'-fucosyllactose and UDP-Gal, illustrating catalytic residues and hydrogen-bonding interactions essential for HMO biosynthesis.
(view all Enzyme-Substrate Complex: 2'-Fucosyllactose and UDP-Gal Binding in Fucosyltransferase)
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