5CO1
Crystal Structure of Zebrafish Protocadherin-19 EC3-4
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 |
| 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-cell adhesion |
| B | 0016020 | cellular_component | membrane |
| 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-cell adhesion |
| C | 0016020 | cellular_component | membrane |
| 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-cell adhesion |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 1001 |
| Chain | Residue |
| A | GLU226 |
| A | ASP282 |
| A | GLU284 |
| A | ASP318 |
| A | HOH1104 |
| A | HOH1108 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 1002 |
| Chain | Residue |
| A | ILE316 |
| A | ASP318 |
| A | ASP354 |
| A | GLU226 |
| A | GLU284 |
| A | ASP315 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 1003 |
| Chain | Residue |
| A | ASN317 |
| A | ASN319 |
| A | ASP352 |
| A | ASP354 |
| A | ASN358 |
| A | ASP404 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 1004 |
| Chain | Residue |
| A | ASP236 |
| A | LEU237 |
| A | THR272 |
| A | HOH1101 |
| A | HOH1109 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 501 |
| Chain | Residue |
| B | GLU226 |
| B | ASP282 |
| B | GLU284 |
| B | ASP318 |
| B | HOH610 |
| B | HOH613 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 502 |
| Chain | Residue |
| B | GLU226 |
| B | GLU284 |
| B | ASP315 |
| B | ILE316 |
| B | ASP318 |
| B | ASP354 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 503 |
| Chain | Residue |
| B | ASN317 |
| B | ASN319 |
| B | ASP352 |
| B | ASP354 |
| B | ASN358 |
| B | ASP404 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 504 |
| Chain | Residue |
| B | ASP236 |
| B | LEU237 |
| B | THR272 |
| B | HOH603 |
| B | HOH608 |
| B | HOH614 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 501 |
| Chain | Residue |
| C | GLU226 |
| C | ASP282 |
| C | GLU284 |
| C | ASP318 |
| C | HOH606 |
| C | HOH611 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 502 |
| Chain | Residue |
| C | GLU226 |
| C | GLU284 |
| C | ASP315 |
| C | ILE316 |
| C | ASP318 |
| C | ASP354 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 503 |
| Chain | Residue |
| C | ASN317 |
| C | ASN319 |
| C | ASP352 |
| C | ASP354 |
| C | ASN358 |
| C | ASP404 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 504 |
| Chain | Residue |
| C | ASP236 |
| C | LEU237 |
| C | THR272 |
| C | HOH608 |
| C | HOH609 |
| C | HOH613 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue CA D 501 |
| Chain | Residue |
| D | GLU226 |
| D | ASP282 |
| D | GLU284 |
| D | ASP318 |
| D | HOH603 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 502 |
| Chain | Residue |
| D | GLU226 |
| D | GLU284 |
| D | ASP315 |
| D | ILE316 |
| D | ASP318 |
| D | ASP354 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 503 |
| Chain | Residue |
| D | ASN317 |
| D | ASN319 |
| D | ASP352 |
| D | ASP354 |
| D | ASN358 |
| D | ASP404 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue CA D 504 |
| Chain | Residue |
| D | ASP236 |
| D | LEU237 |
| D | THR272 |
| D | HOH605 |
| D | HOH609 |
Functional Information from PROSITE/UniProt
| site_id | PS00232 |
| Number of Residues | 11 |
| Details | CADHERIN_1 Cadherin domain signature. VnViDiNDNaP |
| Chain | Residue | Details |
| A | VAL311-PRO321 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27787195","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34520737","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6PGW","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"5IU9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"27787195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5IU9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34520737","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6PGW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 214 |
| Details | Domain: {"description":"Cadherin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00043","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
