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6WMM

Human poly-N-acetyl-lactosamine synthase structure demonstrates a modular assembly of catalytic subsites for GT-A glycosyltransferases

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0005515molecular_functionprotein binding
A0006486biological_processobsolete protein glycosylation
A0008532molecular_functionN-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity
A0009101biological_processglycoprotein biosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016758molecular_functionhexosyltransferase activity
A0018146biological_processkeratan sulfate proteoglycan biosynthetic process
A0030311biological_processpoly-N-acetyllactosamine biosynthetic process
B0000139cellular_componentGolgi membrane
B0005515molecular_functionprotein binding
B0006486biological_processobsolete protein glycosylation
B0008532molecular_functionN-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase activity
B0009101biological_processglycoprotein biosynthetic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016758molecular_functionhexosyltransferase activity
B0018146biological_processkeratan sulfate proteoglycan biosynthetic process
B0030311biological_processpoly-N-acetyllactosamine biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-03-11

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