4BDO
Crystal structure of the GluK2 K531A-T779G LBD dimer in complex with kainate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| A | 0016020 | cellular_component | membrane |
| B | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| B | 0016020 | cellular_component | membrane |
| C | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| C | 0016020 | cellular_component | membrane |
| D | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE KAI A 900 |
| Chain | Residue |
| A | TYR488 |
| A | HOH2037 |
| A | PRO516 |
| A | ALA518 |
| A | ARG523 |
| A | GLY688 |
| A | ALA689 |
| A | THR690 |
| A | ASN721 |
| A | HOH2031 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 902 |
| Chain | Residue |
| A | GLU524 |
| A | ILE527 |
| A | ASP528 |
| B | ASP776 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE KAI B 900 |
| Chain | Residue |
| B | TYR488 |
| B | PRO516 |
| B | ALA518 |
| B | ARG523 |
| B | VAL685 |
| B | GLY688 |
| B | ALA689 |
| B | THR690 |
| B | ASN721 |
| B | HOH2020 |
| B | HOH2021 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 902 |
| Chain | Residue |
| A | ASP776 |
| B | GLU524 |
| B | ILE527 |
| B | ASP528 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE KAI C 900 |
| Chain | Residue |
| C | TYR488 |
| C | PRO516 |
| C | LEU517 |
| C | ALA518 |
| C | ARG523 |
| C | GLY688 |
| C | ALA689 |
| C | THR690 |
| C | ASN721 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 902 |
| Chain | Residue |
| C | GLU524 |
| C | ILE527 |
| C | ASP528 |
| D | ASP776 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE KAI D 900 |
| Chain | Residue |
| D | TYR488 |
| D | PRO516 |
| D | ALA518 |
| D | ARG523 |
| D | VAL685 |
| D | GLY688 |
| D | ALA689 |
| D | THR690 |
| D | ASN721 |
| D | HOH2020 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GLU D 901 |
| Chain | Residue |
| D | TYR488 |
| D | PRO516 |
| D | LEU517 |
| D | ALA518 |
| D | ARG523 |
| D | GLY688 |
| D | ALA689 |
| D | THR690 |
| D | GLU738 |
| D | HOH2020 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 902 |
| Chain | Residue |
| C | ASP776 |
| D | GLU524 |
| D | ILE527 |
| D | ASP528 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| 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 | 4 |
| 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 |
