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2D7R

Crystal structure of pp-GalNAc-T10 complexed with GalNAc-Ser on lectin domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0004653molecular_functionpolypeptide N-acetylgalactosaminyltransferase activity
A0005794cellular_componentGolgi apparatus
A0006486biological_processprotein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0016266biological_processprotein O-linked glycosylation via N-acetyl-galactosamine
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0030246molecular_functioncarbohydrate binding
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues132
DetailsDomain: {"description":"Ricin B-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00174","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues109
DetailsRegion: {"description":"Catalytic subdomain A"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues62
DetailsRegion: {"description":"Catalytic subdomain B"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues11
DetailsRegion: {"description":"Flexible loop"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues11
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16650853","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-10-08

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