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 |
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 | PS00232 |
Number of Residues | 11 |
Details | CADHERIN_1 Cadherin domain signature. IeVqDiNDNtP |
Chain | Residue | Details |
A | ILE99-PRO109 | |
A | VAL211-PRO221 | |
A | VAL318-PRO328 | |
site_id | PS00830 |
Number of Residues | 17 |
Details | GREAB_2 Prokaryotic transcription elongation factors signature 2. SenSPIGhSVIqvkaND |
Chain | Residue | Details |
A | SER233-ASP249 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASN248 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN346 | |