Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 401 |
| Chain | Residue |
| C | ASN102 |
| C | ASN104 |
| C | ASP134 |
| C | ASP136 |
| C | ASN143 |
| C | ASP195 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 402 |
| Chain | Residue |
| C | GLN101 |
| C | ASP103 |
| C | ASP136 |
| C | GLU11 |
| C | GLU69 |
| C | ASP100 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 403 |
| Chain | Residue |
| C | GLU11 |
| C | ASP67 |
| C | GLU69 |
| C | ASP103 |
| C | HOH581 |
| C | HOH698 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue EDO C 404 |
| Chain | Residue |
| C | TRP2 |
| C | TRP2 |
| C | VAL3 |
| C | VAL3 |
| C | ILE4 |
| C | ILE4 |
| C | MET92 |
| C | MET92 |
| C | HOH518 |
| C | HOH518 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 405 |
| Chain | Residue |
| C | GLU13 |
| C | GLY15 |
| C | PRO16 |
| C | LYS19 |
| L | ARG99 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PG4 C 406 |
| Chain | Residue |
| C | ASP138 |
| C | ASN140 |
| C | TYR142 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO H 301 |
| Chain | Residue |
| H | THR90 |
| H | ALA91 |
| H | MET92 |
| H | SER114 |
| H | VAL115 |
| H | THR116 |
| H | HOH416 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO H 302 |
| Chain | Residue |
| H | ARG66 |
| H | SER84 |
| H | GLN86 |
| H | ASP88 |
| H | ASP89 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO H 303 |
| Chain | Residue |
| H | LYS64 |
| H | LEU67 |
| H | HOH424 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO H 304 |
| Chain | Residue |
| C | VAL48 |
| C | GLY49 |
| C | THR63 |
| C | GLU64 |
| H | ARG31 |
| H | TYR104 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO H 305 |
| Chain | Residue |
| H | ASN161 |
| H | SER162 |
| H | ASN202 |
| H | HOH450 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO H 306 |
| Chain | Residue |
| H | GLN111 |
| H | GLY112 |
| H | HOH562 |
| site_id | AD4 |
| Number of Residues | 3 |
| Details | binding site for residue EDO H 307 |
| Chain | Residue |
| H | LEU11 |
| H | HOH431 |
| H | HOH445 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO H 308 |
| Chain | Residue |
| H | SER28 |
| H | LEU29 |
| H | SER30 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue EDO L 301 |
| Chain | Residue |
| H | LEU45 |
| H | GLU46 |
| H | TRP47 |
| H | ASN60 |
| H | HOH511 |
| L | THR103 |
| L | PHE104 |
| L | EDO306 |
| L | HOH405 |
| L | HOH492 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO L 302 |
| Chain | Residue |
| L | SER71 |
| L | GLY72 |
| L | EDO303 |
| L | HOH419 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO L 303 |
| Chain | Residue |
| L | SER58 |
| L | ILE69 |
| L | GLY70 |
| L | EDO302 |
| L | HOH462 |
| L | HOH568 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO L 304 |
| Chain | Residue |
| L | LEU30 |
| L | SER32 |
| L | GLN35 |
| L | HOH415 |
| L | HOH506 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO L 305 |
| Chain | Residue |
| L | LEU30 |
| L | HOH424 |
| L | HOH466 |
| site_id | AE2 |
| Number of Residues | 2 |
| Details | binding site for residue EDO L 306 |
| Chain | Residue |
| L | EDO301 |
| L | PHE104 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO L 307 |
| Chain | Residue |
| L | GLN44 |
| L | PRO46 |
| L | GLY47 |
| L | GLN48 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO L 308 |
| Chain | Residue |
| L | ILE150 |
| L | ASN151 |
| L | VAL152 |
| L | ASN167 |
| L | TRP169 |
Functional Information from PROSITE/UniProt
| site_id | PS00232 |
| Number of Residues | 11 |
| Details | CADHERIN_1 Cadherin domain signature. ItVtDqNDNkP |
| Chain | Residue | Details |
| C | ILE96-PRO106 | |
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
| Chain | Residue | Details |
| L | TYR198-HIS204 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 107 |
| Details | Domain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by S.pyogenes SpeB","evidences":[{"source":"PubMed","id":"23532847","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"UniProtKB","id":"P09803","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"UniProtKB","id":"P09803","evidenceCode":"ECO:0000250"}]} |