4YH7
Crystal structure of PTPdelta ectodomain in complex with IL1RAPL1
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 90 |
| Details | Domain: {"description":"Ig-like C2-type 1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 98 |
| Details | Domain: {"description":"Ig-like C2-type 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 190 |
| Details | Domain: {"description":"Ig-like C2-type 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 90 |
| Details | Domain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 96 |
| Details | Domain: {"description":"Fibronectin type-III 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Region: {"description":"Mini-exon peptide A9; sufficient for interaction with IL1RAPL1","evidences":[{"source":"PubMed","id":"21940441","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Region: {"description":"Mini-exon peptide B; required for interaction with SLITRK2 and in the function in pre-synaptic differentiation; Acts as an adjustable linker to control relative positions and orientations of the PTPRD second and third immunoglobilin domains for their simultaneous interactions with the first immunoglobilin domain of IL1RAPL1 and IL1RAP; Modulates affinity for IL1RAPL1 and IL1RAP","evidences":[{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25989451","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Required for interaction with IL1RAP","evidences":[{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25989451","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4Y61","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YFD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YFG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Site: {"description":"Essential for interaction with PTPRD","evidences":[{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5Y32","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4YH6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YH7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5Y32","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
