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 adhesion via plasma membrane adhesion molecules |
A | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 501 |
Chain | Residue |
A | ASN97 |
A | ASN99 |
A | ASP129 |
A | ASP131 |
A | ASN135 |
A | ASP186 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue CA A 502 |
Chain | Residue |
A | GLU63 |
A | ASP98 |
A | GLU9 |
A | GLU10 |
A | ASP61 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA A 503 |
Chain | Residue |
A | GLU9 |
A | GLU63 |
A | ASP95 |
A | ILE96 |
A | ASP98 |
A | ASP131 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA A 504 |
Chain | Residue |
A | ASN311 |
A | ASN313 |
A | ASP343 |
A | ASP345 |
A | ASN349 |
A | ASP396 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue CA A 505 |
Chain | Residue |
A | GLU223 |
A | GLU280 |
A | ASP309 |
A | GLU310 |
A | ASP312 |
A | ASP345 |
A | CA506 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue CA A 506 |
Chain | Residue |
A | GLU223 |
A | ASP278 |
A | GLU280 |
A | ASP312 |
A | ASN313 |
A | CA505 |
A | HOH609 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue CA A 507 |
Chain | Residue |
A | ASN206 |
A | ASN208 |
A | ASP238 |
A | ASP240 |
A | ASN244 |
A | ASP293 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue CA A 508 |
Chain | Residue |
A | GLU114 |
A | ASP171 |
A | GLU173 |
A | ASP207 |
A | HOH663 |
site_id | AC9 |
Number of Residues | 7 |
Details | binding site for residue CA A 509 |
Chain | Residue |
A | GLU114 |
A | GLU173 |
A | ASP204 |
A | ALA205 |
A | ASP207 |
A | ASN208 |
A | ASP240 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue CL A 510 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue CL A 511 |
site_id | AD3 |
Number of Residues | 3 |
Details | binding site for residue NA A 512 |
Chain | Residue |
A | GLU328 |
A | ASP329 |
A | LEU380 |
site_id | AD4 |
Number of Residues | 8 |
Details | binding site for residue EPE A 513 |
Chain | Residue |
A | SER126 |
A | ASN155 |
A | TYR161 |
A | GLU163 |
A | ILE252 |
A | ASN253 |
A | HOH614 |
A | HOH624 |
site_id | AD5 |
Number of Residues | 1 |
Details | binding site for residue EDO A 514 |
Functional Information from PROSITE/UniProt
site_id | PS00232 |
Number of Residues | 11 |
Details | CADHERIN_1 Cadherin domain signature. VlIqDiNDNpP |
Chain | Residue | Details |
A | VAL91-PRO101 | |
A | VAL200-PRO210 | |
A | ILE305-PRO315 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN106 | |
A | ASN389 | |