12EM
Crystal structure of a B1,3-Glucosyltransferase (B3GLCT) reveals an unusual mode of substrate recognition by a two-domain GT-A fold glycosyltransferase
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 55 |
| Details | Domain: {"description":"TSP type-1 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"C-linked (Man) tryptophan","featureId":"CAR_000210","evidences":[{"source":"PubMed","id":"11067851","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Fuc...) threonine","featureId":"CAR_000211","evidences":[{"source":"PubMed","id":"11067851","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12391027","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
