2D7R
Crystal structure of pp-GalNAc-T10 complexed with GalNAc-Ser on lectin domain
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000139 | cellular_component | Golgi membrane |
A | 0004653 | molecular_function | polypeptide N-acetylgalactosaminyltransferase activity |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0006486 | biological_process | protein glycosylation |
A | 0006493 | biological_process | protein O-linked glycosylation |
A | 0016266 | biological_process | protein O-linked glycosylation via N-acetyl-galactosamine |
A | 0016740 | molecular_function | transferase activity |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 132 |
Details | Domain: {"description":"Ricin B-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00174","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 109 |
Details | Region: {"description":"Catalytic subdomain A"} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 62 |
Details | Region: {"description":"Catalytic subdomain B"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 11 |
Details | Region: {"description":"Flexible loop"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 11 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16650853","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |