4OY9
Crystal structure of human P-Cadherin EC1-EC2 in closed conformation
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 401 |
| Chain | Residue |
| A | ASN102 |
| A | HIS104 |
| A | ASP134 |
| A | ASP136 |
| A | ASN143 |
| A | ASP195 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 402 |
| Chain | Residue |
| A | GLN101 |
| A | ASP103 |
| A | ASP136 |
| A | GLU11 |
| A | GLU69 |
| A | ASP100 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 403 |
| Chain | Residue |
| A | GLU11 |
| A | ASP67 |
| A | GLU69 |
| A | ASP103 |
| A | HOH697 |
| A | HOH698 |
Functional Information from PROSITE/UniProt
| site_id | PS00232 |
| Number of Residues | 11 |
| Details | CADHERIN_1 Cadherin domain signature. IiVtDqNDHkP |
| Chain | Residue | Details |
| A | ILE96-PRO106 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 107 |
| 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 | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
