3FVC
Crystal structure of a trimeric variant of the Epstein-Barr virus glycoprotein B
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | Region: {"description":"Involved in fusion and/or binding to host membrane","evidences":[{"source":"HAMAP-Rule","id":"MF_04032","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04032","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04032","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19196955","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
