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8ZX3

Structure-Based Mechanism and Specificity of Human Galactosyltransferase B3GalT5

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0006486biological_processprotein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0006629biological_processlipid metabolic process
A0008499molecular_functionN-acetyl-beta-D-glucosaminide beta-(1,3)-galactosyltransferase activity
A0009312biological_processoligosaccharide biosynthetic process
A0009617biological_processresponse to bacterium
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A1901137biological_processcarbohydrate derivative biosynthetic process
B0000139cellular_componentGolgi membrane
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0006486biological_processprotein glycosylation
B0006493biological_processprotein O-linked glycosylation
B0006629biological_processlipid metabolic process
B0008499molecular_functionN-acetyl-beta-D-glucosaminide beta-(1,3)-galactosyltransferase activity
B0009312biological_processoligosaccharide biosynthetic process
B0009617biological_processresponse to bacterium
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B1901137biological_processcarbohydrate derivative biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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