Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0005509 | molecular_function | calcium ion binding | 
| A | 0005886 | cellular_component | plasma membrane | 
| A | 0007155 | biological_process | cell adhesion | 
| A | 0007156 | biological_process | homophilic cell-cell adhesion | 
| A | 0016020 | cellular_component | membrane | 
| A | 0098609 | biological_process | cell-cell adhesion | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE CA A 401 | 
| Chain | Residue | 
| A | ASN4 | 
| A | ARG5 | 
| A | ASP37 | 
| A | ASP39 | 
| A | ASP41 | 
| A | ASP87 | 
| site_id | AC2 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE CA A 402 | 
| Chain | Residue | 
| A | VAL103 | 
| A | ASP105 | 
| A | ASP138 | 
| A | GLU22 | 
| A | GLU74 | 
| A | ASP102 | 
| site_id | AC3 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE CA A 403 | 
| Chain | Residue | 
| A | ASN104 | 
| A | ASN106 | 
| A | ASP136 | 
| A | ASP138 | 
| A | GLY142 | 
| A | ASP187 | 
| site_id | AC4 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE NA A 501 | 
| Chain | Residue | 
| A | GLU22 | 
| A | ASP72 | 
| A | GLU74 | 
| A | ASP105 | 
| A | GOL1002 | 
| A | HOH2141 | 
| site_id | AC5 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE NA A 502 | 
| Chain | Residue | 
| A | VAL47 | 
| A | SER53 | 
| A | HOH2102 | 
| A | HOH2105 | 
| A | HOH2108 | 
| A | HOH2119 | 
| site_id | AC6 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE NA A 503 | 
| Chain | Residue | 
| A | ASP136 | 
| A | GLY143 | 
| A | HOH2208 | 
| A | HOH2209 | 
| A | HOH2211 | 
| A | HOH2214 | 
| site_id | AC7 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE CL A 601 | 
| Chain | Residue | 
| A | PHE9 | 
| A | ILE92 | 
| A | ASN122 | 
| A | HOH2166 | 
| A | HOH2190 | 
| site_id | AC8 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE GOL A 1001 | 
| Chain | Residue | 
| A | ASP102 | 
| A | ASN104 | 
| A | LEU139 | 
| A | GLY142 | 
| A | ASP189 | 
| A | LYS190 | 
| A | HOH2258 | 
| site_id | AC9 | 
| Number of Residues | 11 | 
| Details | BINDING SITE FOR RESIDUE GOL A 1002 | 
| Chain | Residue | 
| A | GLU22 | 
| A | PRO70 | 
| A | LEU71 | 
| A | ASP72 | 
| A | VAL103 | 
| A | ASP105 | 
| A | NA501 | 
| A | HOH2259 | 
| A | HOH2260 | 
| A | HOH2261 | 
| A | HOH2262 | 
Functional Information from PROSITE/UniProt
| site_id | PS00232 | 
| Number of Residues | 11 | 
| Details | CADHERIN_1 Cadherin domain signature. IqVgDvNDNaP | 
| Chain | Residue | Details | 
| A | ILE98-PRO108 |  | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 98 | 
| Details | Domain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]} | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 2 | 
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |