Literature summary for 2.4.1.41 extracted from

Yu, C.; Liang, L.; Yin, Y.
Structural basis of carbohydrate transfer activity of UDP-GalNAc Polypeptide N-acetylgalactosaminyltransferase 7 (2019), Biochem. Biophys. Res. Commun., 510, 266-271 .

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of GalNAc-T7, and of its complex with the donor substrate UDP-GalNAc. The N-terminal catalytic domain and C-terminal lectin domain are connected by a flexible linker, forming a narrow cleft for the acceptor substrate. Only the alpha subdomain of the lectin domain binds to the glycosyl group. Compared to the apo structure, the loop covering the catalytic center of the complex show significant conformational changes	Homo sapiens

Crystallization (Comment)

Organism

structures of GalNAc-T7, and of its complex with the donor substrate UDP-GalNAc. The N-terminal catalytic domain and C-terminal lectin domain are connected by a flexible linker, forming a narrow cleft for the acceptor substrate. Only the alpha subdomain of the lectin domain binds to the glycosyl group. Compared to the apo structure, the loop covering the catalytic center of the complex show significant conformational changes

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q86SF2	isoform GALNT7	-

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Release 2023.1 (January 2023)