3O29
Ligand-binding domain of GluA2 (flip) ionotropic glutamate receptor in complex with an allosteric modulator
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE GLU A 264 |
| Chain | Residue |
| A | TYR61 |
| A | GLU193 |
| A | HOH272 |
| A | HOH276 |
| A | HOH294 |
| A | PRO89 |
| A | LEU90 |
| A | THR91 |
| A | ARG96 |
| A | LEU138 |
| A | GLY141 |
| A | SER142 |
| A | THR143 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 265 |
| Chain | Residue |
| A | GLU24 |
| A | ARG31 |
| A | HIS46 |
| A | LYS240 |
| A | GLN244 |
| A | HOH275 |
| A | HOH467 |
| A | HOH507 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 266 |
| Chain | Residue |
| A | ASP139 |
| A | SER140 |
| A | LYS144 |
| A | ARG148 |
| A | HOH339 |
| A | HOH406 |
| A | HOH442 |
| A | HOH443 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 267 |
| Chain | Residue |
| A | GLY62 |
| A | ALA63 |
| A | TRP71 |
| A | THR93 |
| A | VAL95 |
| A | ARG96 |
| A | HOH278 |
| A | HOH368 |
| A | HOH442 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 268 |
| Chain | Residue |
| A | GLU97 |
| A | ASP101 |
| A | PHE102 |
| A | LYS104 |
| A | HOH460 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 269 |
| Chain | Residue |
| A | TRP159 |
| A | ARG163 |
| A | HOH465 |
| A | HOH493 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 270 |
| Chain | Residue |
| A | ASN214 |
| A | ASP216 |
| A | SER217 |
| A | ASP248 |
| site_id | AC8 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE O29 A 271 |
| Chain | Residue |
| A | ILE92 |
| A | PRO105 |
| A | PRO105 |
| A | PHE106 |
| A | PHE106 |
| A | MET107 |
| A | SER108 |
| A | SER108 |
| A | SER217 |
| A | SER217 |
| A | LYS218 |
| A | LYS218 |
| A | GLY219 |
| A | GLY219 |
| A | LEU239 |
| A | SER242 |
| A | LEU247 |
| A | ASP248 |
| A | HOH316 |
| A | HOH318 |
| A | HOH411 |
| A | HOH412 |
| A | HOH413 |
| A | HOH503 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| 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 | 3 |
| 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 | 1 |
| 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 | 1 |
| 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 | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"PubMed","id":"8848293","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
