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-cell adhesion |
| A | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue EPE A 501 |
| Chain | Residue |
| A | GLU155 |
| A | TRP186 |
| A | TYR189 |
| A | ASP190 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | GLU9 |
| A | GLU10 |
| A | ASP59 |
| A | GLU61 |
| A | ASP106 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 503 |
| Chain | Residue |
| A | GLU9 |
| A | GLU61 |
| A | ASP103 |
| A | ILE104 |
| A | ASP106 |
| A | ASP139 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 504 |
| Chain | Residue |
| A | ASN105 |
| A | ASN107 |
| A | ASP137 |
| A | ASP139 |
| A | ASN143 |
| A | ASP197 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 505 |
| Chain | Residue |
| A | GLU122 |
| A | ASP182 |
| A | GLU184 |
| A | ASP218 |
| A | HOH601 |
| A | HOH611 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 506 |
| Chain | Residue |
| A | GLU122 |
| A | GLU184 |
| A | ASP215 |
| A | THR216 |
| A | ASP218 |
| A | ASP251 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 507 |
| Chain | Residue |
| A | ASN217 |
| A | ASN219 |
| A | ASP249 |
| A | ASP251 |
| A | ASN255 |
| A | ASP304 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 508 |
| Chain | Residue |
| A | GLU234 |
| A | ASP289 |
| A | GLU291 |
| A | ASP325 |
| A | ASN326 |
| A | HOH603 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 509 |
| Chain | Residue |
| A | GLU234 |
| A | GLU291 |
| A | ASP322 |
| A | MET323 |
| A | ASP325 |
| A | ASP366 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 510 |
| Chain | Residue |
| A | ASN324 |
| A | ASN326 |
| A | ASP364 |
| A | ASP366 |
| A | ASN370 |
| A | ASP423 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 511 |
| Chain | Residue |
| A | GLU349 |
| A | ASP408 |
| A | ASP441 |
| A | VAL442 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 512 |
| Chain | Residue |
| A | ASP187 |
| A | SER188 |
| A | GLU369 |
| A | SER424 |
| A | ASN426 |
Functional Information from PROSITE/UniProt
| site_id | PS00830 |
| Number of Residues | 17 |
| Details | GREAB_2 Prokaryotic transcription elongation factors signature 2. SenSPIGhSVIqvkaND |
| Chain | Residue | Details |
| A | SER233-ASP249 | |
| site_id | PS00232 |
| Number of Residues | 11 |
| Details | CADHERIN_1 Cadherin domain signature. IeVqDiNDNtP |
| Chain | Residue | Details |
| A | ILE99-PRO109 | |
| A | VAL211-PRO221 | |
| A | VAL318-PRO328 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 111 |
| Details | Domain: {"description":"Cadherin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 106 |
| Details | Domain: {"description":"Cadherin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
