Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| 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 | 0007156 | biological_process | homophilic cell-cell adhesion |
| B | 0016020 | cellular_component | membrane |
| B | 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 | ASP67 |
| A | GLU69 |
| A | ASP103 |
| A | HOH431 |
| A | HOH500 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 302 |
| Chain | Residue |
| A | GLN101 |
| A | ASP103 |
| A | ASP136 |
| A | GLU11 |
| A | GLU69 |
| A | ASP100 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 303 |
| Chain | Residue |
| A | ASN102 |
| A | HIS104 |
| A | ASP134 |
| A | ASP136 |
| A | ASN143 |
| A | ASP195 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 304 |
| Chain | Residue |
| A | GLU69 |
| A | HOH444 |
| B | GLN129 |
| B | HOH496 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CA A 305 |
| Chain | Residue |
| A | ASP199 |
| A | ASP213 |
| A | HOH503 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue 1PE A 306 |
| Chain | Residue |
| A | GLY124 |
| A | HIS151 |
| A | THR164 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 301 |
| Chain | Residue |
| B | GLU11 |
| B | ASP67 |
| B | GLU69 |
| B | ASP103 |
| B | HOH420 |
| B | HOH484 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 302 |
| Chain | Residue |
| B | GLU11 |
| B | GLU69 |
| B | ASP100 |
| B | GLN101 |
| B | ASP103 |
| B | ASP136 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 303 |
| Chain | Residue |
| B | ASN102 |
| B | HIS104 |
| B | ASP134 |
| B | ASP136 |
| B | ASN143 |
| B | ASP195 |
Functional Information from PROSITE/UniProt
| site_id | PS00232 |
| Number of Residues | 11 |
| Details | CADHERIN_1 Cadherin domain signature. IiVtDqNDHkP |
| Chain | Residue | Details |
| A | ILE96-PRO106 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 107 |
| Details | Domain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]} |
