Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016020 | cellular_component | membrane |
| A | 0051260 | biological_process | protein homooligomerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 1232 |
| Chain | Residue |
| A | PHE141 |
| A | GLY142 |
| A | ASN143 |
| A | GLU146 |
| A | LYS204 |
| A | ARG208 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GSH A 1231 |
| Chain | Residue |
| A | TYR145 |
| A | CYS148 |
| A | TYR149 |
| A | TYR150 |
| A | MET154 |
| A | HOH2015 |
| A | HOH2017 |
| A | ARG136 |
| A | PRO137 |
| A | LEU138 |
Functional Information from PROSITE/UniProt
| site_id | PS00706 |
| Number of Residues | 19 |
| Details | PRION_2 Prion protein signature 2. EtDiKIMeRVVeQMCitQY |
| Chain | Residue | Details |
| A | GLU200-TYR218 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Lipidation: {"description":"GPI-anchor amidated alanine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"33600485","evidenceCode":"ECO:0000269"}]} |