Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005509 | molecular_function | calcium ion binding |
A | 0007156 | biological_process | homophilic cell adhesion via plasma membrane adhesion molecules |
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 adhesion via plasma membrane adhesion molecules |
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 | ASN102 |
A | HIS104 |
A | ASP134 |
A | ASP136 |
A | ASN143 |
A | ASP195 |
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 | 3 |
Details | binding site for residue NI A 303 |
Chain | Residue |
A | HIS104 |
A | SO4305 |
A | SO4306 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue NI A 304 |
Chain | Residue |
A | MET0 |
B | MET0 |
B | HOH404 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue SO4 A 305 |
Chain | Residue |
A | ASP67 |
A | GLU69 |
A | HIS104 |
A | GLU135 |
A | NI303 |
A | SO4306 |
site_id | AC6 |
Number of Residues | 5 |
Details | binding site for residue SO4 A 306 |
Chain | Residue |
A | ASP67 |
A | ASP103 |
A | HIS104 |
A | NI303 |
A | SO4305 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue GOL A 307 |
Chain | Residue |
A | ASP197 |
A | ASP199 |
B | ASN12 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue CA B 301 |
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 302 |
Chain | Residue |
B | ASN102 |
B | HIS104 |
B | ASP134 |
B | ASP136 |
B | ASN143 |
B | ASP195 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue NI B 303 |
Chain | Residue |
B | HIS104 |
B | SO4304 |
B | SO4305 |
B | HOH401 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 304 |
Chain | Residue |
B | ASP67 |
B | ASP103 |
B | HIS104 |
B | NI303 |
B | SO4305 |
B | HOH401 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue SO4 B 305 |
Chain | Residue |
B | ASP67 |
B | HIS104 |
B | GLU135 |
B | NI303 |
B | SO4304 |
B | HOH401 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue GOL B 306 |
Chain | Residue |
A | ASN12 |
B | MET196 |
B | ASP199 |
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 | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN93 | |
B | ASN93 | |