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4YFD

Crystal structure PTP delta Ig1-Fn2 in complex with IL-1RAcP

Functional Information from GO Data
ChainGOidnamespacecontents
B0004908molecular_functioninterleukin-1 receptor activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues189
DetailsDomain: {"description":"Ig-like C2-type 2"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsRegion: {"description":"Essential for interaction with PTPRD","evidences":[{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4YFD","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues90
DetailsDomain: {"description":"Ig-like C2-type 1"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues82
DetailsDomain: {"description":"Ig-like C2-type 3"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues90
DetailsDomain: {"description":"Fibronectin type-III 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00316","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsRegion: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues3
DetailsRegion: {"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"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsSite: {"description":"Required for interaction with IL1RAP","evidences":[{"source":"PubMed","id":"25908590","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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