4NUM
Crystal structure of mouse N-cadherin EC1-2 A78SI92M
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 |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007155 | biological_process | cell adhesion |
| B | 0007156 | biological_process | homophilic cell adhesion via plasma membrane adhesion molecules |
| B | 0016020 | cellular_component | membrane |
| B | 0098609 | biological_process | cell-cell adhesion |
| 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 adhesion via plasma membrane adhesion molecules |
| C | 0016020 | cellular_component | membrane |
| C | 0098609 | biological_process | cell-cell adhesion |
| D | 0005509 | molecular_function | calcium ion binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0007155 | biological_process | cell adhesion |
| D | 0007156 | biological_process | homophilic cell adhesion via plasma membrane adhesion molecules |
| D | 0016020 | cellular_component | membrane |
| D | 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 | ASN104 |
| A | ASP134 |
| A | ASP136 |
| A | ASN142 |
| A | ASP194 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 302 |
| Chain | Residue |
| A | MET101 |
| A | ASP103 |
| A | ASP136 |
| A | GLU11 |
| A | GLU69 |
| A | ASP100 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 303 |
| Chain | Residue |
| A | GLU11 |
| A | ASP67 |
| A | GLU69 |
| A | ASP103 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 301 |
| Chain | Residue |
| B | ASN102 |
| B | ASN104 |
| B | ASP134 |
| B | ASP136 |
| B | ASN142 |
| B | ASP194 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 302 |
| Chain | Residue |
| B | GLU11 |
| B | GLU69 |
| B | ASP100 |
| B | MET101 |
| B | ASP103 |
| B | ASP136 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 303 |
| Chain | Residue |
| B | GLU11 |
| B | ASN12 |
| B | ASP67 |
| B | GLU69 |
| B | ASP103 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 301 |
| Chain | Residue |
| C | ASN102 |
| C | ASN104 |
| C | ASP134 |
| C | ASP136 |
| C | ASN142 |
| C | ASP194 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 302 |
| Chain | Residue |
| C | GLU11 |
| C | GLU69 |
| C | ASP100 |
| C | MET101 |
| C | ASP103 |
| C | ASP136 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA C 303 |
| Chain | Residue |
| C | GLU11 |
| C | ASP67 |
| C | GLU69 |
| C | ASP103 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 301 |
| Chain | Residue |
| D | ASN102 |
| D | ASN104 |
| D | ASP134 |
| D | ASP136 |
| D | ASN142 |
| D | ASP194 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 302 |
| Chain | Residue |
| D | GLU11 |
| D | GLU69 |
| D | ASP100 |
| D | MET101 |
| D | ASP103 |
| D | ASP136 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 303 |
| Chain | Residue |
| D | GLU11 |
| D | ASP67 |
| D | GLU69 |
| D | ASP103 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 428 |
| Details | Domain: {"description":"Cadherin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25253890","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NUQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21366346","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25253890","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4NUQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21300292","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3Q2W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
