3Q2W
Crystal structure of mouse N-cadherin ectodomain
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 |
A | 0098609 | biological_process | cell-cell adhesion |
Functional Information from PROSITE/UniProt
site_id | PS00232 |
Number of Residues | 11 |
Details | CADHERIN_1 Cadherin domain signature. InViDmNDNrP |
Chain | Residue | Details |
A | ILE96-PRO106 | |
A | ILE211-PRO221 | |
A | ILE434-PRO444 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:25253890, ECO:0007744|PDB:4NUQ |
Chain | Residue | Details |
A | GLU11 | |
A | ASP194 | |
A | ASP67 | |
A | GLU69 | |
A | ASP100 | |
A | MET101 | |
A | ASN102 | |
A | ASN104 | |
A | ASP136 | |
A | ASN142 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21366346, ECO:0000269|PubMed:25253890, ECO:0007744|PDB:4NUQ |
Chain | Residue | Details |
A | ASP103 | |
A | ASP134 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN31 | |
A | ASN533 |
site_id | SWS_FT_FI4 |
Number of Residues | 5 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21300292, ECO:0007744|PDB:3Q2W |
Chain | Residue | Details |
A | ASN114 | |
A | ASN166 | |
A | ASN243 | |
A | ASN413 | |
A | ASN492 |