8FWU
Structure of the ligand-binding and transmembrane domains of kainate receptor GluK2 in complex with the positive allosteric modulator BPAM344 and competitive antagonist DNQX
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005216 | molecular_function | monoatomic ion channel activity |
A | 0006811 | biological_process | monoatomic ion transport |
A | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
A | 0016020 | cellular_component | membrane |
A | 0038023 | molecular_function | signaling receptor activity |
B | 0005216 | molecular_function | monoatomic ion channel activity |
B | 0006811 | biological_process | monoatomic ion transport |
B | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
B | 0016020 | cellular_component | membrane |
B | 0038023 | molecular_function | signaling receptor activity |
C | 0005216 | molecular_function | monoatomic ion channel activity |
C | 0006811 | biological_process | monoatomic ion transport |
C | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
C | 0016020 | cellular_component | membrane |
C | 0038023 | molecular_function | signaling receptor activity |
D | 0005216 | molecular_function | monoatomic ion channel activity |
D | 0006811 | biological_process | monoatomic ion transport |
D | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
D | 0016020 | cellular_component | membrane |
D | 0038023 | molecular_function | signaling receptor activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 240 |
Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 220 |
Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"8163463","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 636 |
Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"8163463","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
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_FI5 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"UniProtKB","id":"Q13002","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
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 |