Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| A | 0051260 | biological_process | protein homooligomerization |
| B | 0016020 | cellular_component | membrane |
| B | 0051260 | biological_process | protein homooligomerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CD B 300 |
| Chain | Residue |
| A | HIS140 |
| A | ASP147 |
| A | HOH324 |
| B | ASN173 |
| B | HIS177 |
| B | HOH409 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CD B 301 |
| Chain | Residue |
| B | ASP147 |
| B | HOH468 |
| A | HIS177 |
| A | HOH325 |
| B | HIS140 |
Functional Information from PROSITE/UniProt
| site_id | PS00291 |
| Number of Residues | 16 |
| Details | PRION_1 Prion protein signature 1. AGAAAAGAVVGGLGGY |
| Chain | Residue | Details |
| A | ALA113-TYR128 | |
| site_id | PS00706 |
| Number of Residues | 19 |
| Details | PRION_2 Prion protein signature 2. EtDvKMMeRVVeQMCitQY |
| Chain | Residue | Details |
| A | GLU200-TYR218 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12214108","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]} |
