2XXT
Crystal structure of the GluK2 (GluR6) wild-type LBD dimer in complex with kainate
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE KAI A 900 |
Chain | Residue |
A | GLU440 |
A | GLU738 |
A | HOH2115 |
A | HOH2146 |
A | HOH2161 |
A | TYR488 |
A | PRO516 |
A | ALA518 |
A | ARG523 |
A | GLY688 |
A | ALA689 |
A | THR690 |
A | ASN721 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 901 |
Chain | Residue |
A | LYS531 |
A | HOH2191 |
B | LYS531 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 902 |
Chain | Residue |
A | GLU524 |
A | ILE527 |
A | ASP528 |
A | HOH2093 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE KAI B 900 |
Chain | Residue |
B | GLU440 |
B | TYR488 |
B | PRO516 |
B | ALA518 |
B | ARG523 |
B | GLY688 |
B | ALA689 |
B | THR690 |
B | ASN721 |
B | GLU738 |
B | HOH2098 |
B | HOH2145 |
B | HOH2199 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA B 902 |
Chain | Residue |
B | GLU524 |
B | ILE527 |
B | ASP528 |
B | HOH2076 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15721240","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17115050","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1S50","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1S7Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2I0B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2I0C","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15677325","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8163463","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |