5KCA
Crystal structure of the Cbln1 C1q domain trimer in complex with the amino-terminal domain (ATD) of iGluR Delta-2 (GluD2)
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | binding site for residue CA A 1001 |
Chain | Residue |
A | GLU734 |
A | ASN736 |
A | VAL760 |
A | ARG761 |
A | SER763 |
A | TYR891 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 321 |
Details | Region: {"description":"Interaction with CBLN1 homotrimer","evidences":[{"source":"PubMed","id":"27418511","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Site: {"description":"Essential for dimerization","evidences":[{"source":"PubMed","id":"27418511","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 131 |
Details | Region: {"description":"Necessary for interaction with CBLN3, and homotrimerization","evidences":[{"source":"UniProtKB","id":"Q9R171","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 25 |
Details | Region: {"description":"Essential for interaction with GRID2","evidences":[{"source":"PubMed","id":"27418511","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"27418511","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5KC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5KC6","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |