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8AY1

Crystal structure of the C. elegans POFUT2 (CePoFUT2) triple mutant (R298K-R299K-A418C) in complex with the Rattus norvegicus TSR4 single mutant (E10C) from F-spondin

Functional Information from GO Data
ChainGOidnamespacecontents
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0036066biological_processprotein O-linked glycosylation via fucose
A0046922molecular_functionpeptide-O-fucosyltransferase activity
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0036066biological_processprotein O-linked glycosylation via fucose
B0046922molecular_functionpeptide-O-fucosyltransferase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9Y2G5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26854667","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5FOE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"description":"Essential for catalytic activity","evidences":[{"source":"UniProtKB","id":"Q9Y2G5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17761667","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26854667","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2026-03-25

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