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 |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007155 | biological_process | cell adhesion |
| B | 0007156 | biological_process | homophilic cell-cell adhesion |
| B | 0016020 | cellular_component | membrane |
| B | 0098609 | biological_process | cell-cell adhesion |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0007155 | biological_process | cell adhesion |
| C | 0007156 | biological_process | homophilic cell-cell adhesion |
| C | 0016020 | cellular_component | membrane |
| C | 0098609 | biological_process | cell-cell adhesion |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0007155 | biological_process | cell adhesion |
| D | 0007156 | biological_process | homophilic cell-cell adhesion |
| D | 0016020 | cellular_component | membrane |
| D | 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 301 |
| Chain | Residue |
| A | GLU11 |
| A | GLU12 |
| A | ASP64 |
| A | GLU66 |
| A | ASP101 |
| A | HOH563 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 302 |
| Chain | Residue |
| A | ILE99 |
| A | ASP101 |
| A | ASP134 |
| A | GLU11 |
| A | GLU66 |
| A | ASP98 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 303 |
| Chain | Residue |
| A | ASN100 |
| A | ASN102 |
| A | ASP132 |
| A | ASP134 |
| A | SER141 |
| A | ASP187 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 301 |
| Chain | Residue |
| B | ASN100 |
| B | ASN102 |
| B | ASP132 |
| B | ASP134 |
| B | SER141 |
| B | ASP187 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 302 |
| Chain | Residue |
| B | GLU11 |
| B | GLU66 |
| B | ASP98 |
| B | ILE99 |
| B | ASP101 |
| B | ASP134 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 303 |
| Chain | Residue |
| B | GLU11 |
| B | GLU12 |
| B | ASP64 |
| B | GLU66 |
| B | ASP101 |
| B | HOH621 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CA C 301 |
| Chain | Residue |
| C | ASN170 |
| C | ARG173 |
| C | ASN175 |
| C | HOH606 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 302 |
| Chain | Residue |
| C | GLU11 |
| C | GLU66 |
| C | ASP98 |
| C | ILE99 |
| C | ASP101 |
| C | ASP134 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 303 |
| Chain | Residue |
| C | GLU11 |
| C | GLU12 |
| C | ASP64 |
| C | GLU66 |
| C | ASP101 |
| C | HOH617 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 304 |
| Chain | Residue |
| C | ASN100 |
| C | ASN102 |
| C | ASP132 |
| C | ASP134 |
| C | SER141 |
| C | ASP187 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 301 |
| Chain | Residue |
| D | GLU11 |
| D | GLU66 |
| D | ASP98 |
| D | ILE99 |
| D | ASP101 |
| D | ASP134 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 302 |
| Chain | Residue |
| D | ASN100 |
| D | ASN102 |
| D | ASP132 |
| D | ASP134 |
| D | SER141 |
| D | ASP187 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 303 |
| Chain | Residue |
| D | GLU11 |
| D | GLU12 |
| D | ASP64 |
| D | GLU66 |
| D | ASP101 |
| D | HOH546 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue CA D 304 |
| Chain | Residue |
| D | GLU117 |
| D | ASP172 |
| D | ASN175 |
Functional Information from PROSITE/UniProt
| site_id | PS00232 |
| Number of Residues | 11 |
| Details | CADHERIN_1 Cadherin domain signature. IkIhDiNDNeP |
| Chain | Residue | Details |
| A | ILE94-PRO104 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 420 |
| Details | Domain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |