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 |
C | 0005509 | molecular_function | calcium ion binding |
C | 0007156 | biological_process | homophilic cell adhesion via plasma membrane adhesion molecules |
C | 0016020 | cellular_component | membrane |
C | 0098609 | biological_process | cell-cell adhesion |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue CA A 301 |
Chain | Residue |
A | GLU11 |
A | ASP67 |
A | GLU69 |
A | ASP103 |
A | HOH411 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue CA A 302 |
Chain | Residue |
A | ASP103 |
A | ASP136 |
A | GLU11 |
A | GLU69 |
A | ASP100 |
A | GLN101 |
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 | 2 |
Details | binding site for residue CA A 304 |
Chain | Residue |
A | ASP44 |
A | HOH433 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CA C 301 |
Chain | Residue |
C | GLU11 |
C | GLU69 |
C | ASP100 |
C | GLN101 |
C | ASP103 |
C | ASP136 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CA C 302 |
Chain | Residue |
C | ASN102 |
C | HIS104 |
C | ASP134 |
C | ASP136 |
C | ASN143 |
C | ASP195 |
site_id | AC7 |
Number of Residues | 6 |
Details | binding site for residue CA C 303 |
Chain | Residue |
C | GLU11 |
C | ASP67 |
C | GLU69 |
C | ASP103 |
C | HOH408 |
C | HOH433 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue CA C 304 |
Chain | Residue |
C | THR109 |
D | HOH308 |
D | HOH313 |
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 | |
C | ASN93 | |