3IK6
Crystal structure of the AMPA subunit GluR2 bound to the allosteric modulator, chlorothiazide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| B | 0016020 | cellular_component | membrane |
| E | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| E | 0016020 | cellular_component | membrane |
| H | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| H | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HCZ B 800 |
| Chain | Residue |
| B | LYS104 |
| E | SER217 |
| E | LYS218 |
| E | GLY219 |
| E | HOH319 |
| B | PRO105 |
| B | SER108 |
| B | LEU239 |
| B | SER242 |
| B | HCZ262 |
| E | ILE92 |
| E | PRO105 |
| E | SER108 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE HCZ B 262 |
| Chain | Residue |
| B | ILE92 |
| B | PRO105 |
| B | SER108 |
| B | LYS218 |
| B | GLY219 |
| B | HCZ800 |
| E | LYS104 |
| E | PRO105 |
| E | SER108 |
| E | LEU239 |
| E | HOH291 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 2 |
| Chain | Residue |
| B | GLU42 |
| B | HIS46 |
| B | HOH482 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN E 3 |
| Chain | Residue |
| E | GLU42 |
| E | HIS46 |
| H | GLU166 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN E 262 |
| Chain | Residue |
| B | ASP65 |
| B | HOH487 |
| E | HIS23 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HCZ H 800 |
| Chain | Residue |
| H | ILE92 |
| H | PRO105 |
| H | PRO105 |
| H | SER108 |
| H | SER108 |
| H | SER217 |
| H | LYS218 |
| H | GLY219 |
| H | LEU239 |
| H | SER242 |
| H | HOH286 |
| H | HOH343 |
| H | HOH422 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN H 1 |
| Chain | Residue |
| E | GLU166 |
| H | GLU42 |
| H | LYS45 |
| H | HIS46 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN H 2 |
| Chain | Residue |
| B | HIS23 |
| H | HIS23 |
| H | GLU30 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11086992","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16483599","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FTJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CMO","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Site: {"description":"Interaction with the cone snail toxin Con-ikot-ikot","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Site: {"description":"Crucial to convey clamshell closure to channel opening","evidences":[{"source":"PubMed","id":"25103405","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
