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2WNB

Crystal Structure of a Mammalian Sialyltransferase in complex with disaccharide and CMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0006486biological_processprotein glycosylation
A0008373molecular_functionsialyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19820709","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 340
ChainResidueDetails
AASP285hydrogen bond acceptor, steric role
AASN335activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2025-07-30

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