5OEW
Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with glutamate and positive allosteric modulator BPAM538
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue GLU A 301 |
| Chain | Residue |
| A | TYR61 |
| A | HOH434 |
| A | HOH442 |
| A | HOH447 |
| A | PRO89 |
| A | LEU90 |
| A | THR91 |
| A | ARG96 |
| A | GLY141 |
| A | SER142 |
| A | THR143 |
| A | GLU193 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 302 |
| Chain | Residue |
| A | GLU42 |
| A | HIS46 |
| A | HOH546 |
| C | GLU166 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue ZN A 303 |
| Chain | Residue |
| A | ASP126 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue ZN A 304 |
| Chain | Residue |
| A | HOH407 |
| A | HOH411 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue ACT A 305 |
| Chain | Residue |
| A | ASP216 |
| A | SER217 |
| B | ASP248 |
| site_id | AC6 |
| Number of Residues | 26 |
| Details | binding site for residue 9TE B 901 |
| Chain | Residue |
| A | LYS104 |
| A | PRO105 |
| A | PHE106 |
| A | MET107 |
| A | SER108 |
| A | SER217 |
| A | LYS218 |
| A | GLY219 |
| A | ASN242 |
| A | LEU247 |
| A | HOH416 |
| A | HOH470 |
| A | HOH553 |
| A | HOH554 |
| B | LYS104 |
| B | PRO105 |
| B | PHE106 |
| B | MET107 |
| B | SER108 |
| B | SER217 |
| B | LYS218 |
| B | GLY219 |
| B | ASN242 |
| B | LEU247 |
| B | HOH1053 |
| B | HOH1069 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | binding site for residue GLU B 902 |
| Chain | Residue |
| B | TYR61 |
| B | PRO89 |
| B | LEU90 |
| B | THR91 |
| B | ARG96 |
| B | LEU138 |
| B | GLY141 |
| B | SER142 |
| B | THR143 |
| B | GLU193 |
| B | HOH1015 |
| B | HOH1043 |
| B | HOH1061 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 903 |
| Chain | Residue |
| B | GLU42 |
| B | LYS45 |
| B | HIS46 |
| B | HOH1063 |
| B | HOH1140 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 904 |
| Chain | Residue |
| B | ASP139 |
| B | HOH1017 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 905 |
| Chain | Residue |
| B | ASP156 |
| B | HOH1052 |
| B | HOH1124 |
| B | HOH1133 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue ZN B 906 |
| Chain | Residue |
| B | ASP65 |
| B | ACT909 |
| B | HOH1122 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 907 |
| Chain | Residue |
| B | HIS46 |
| B | HOH1158 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 908 |
| Chain | Residue |
| B | HOH1006 |
| B | HOH1007 |
| site_id | AD5 |
| Number of Residues | 4 |
| Details | binding site for residue ACT B 909 |
| Chain | Residue |
| B | ASP65 |
| B | ASP67 |
| B | ZN906 |
| B | HOH1008 |
| site_id | AD6 |
| Number of Residues | 18 |
| Details | binding site for residue 9TE C 301 |
| Chain | Residue |
| C | HOH402 |
| C | HOH403 |
| C | LYS104 |
| C | PRO105 |
| C | PRO105 |
| C | PHE106 |
| C | PHE106 |
| C | MET107 |
| C | MET107 |
| C | SER108 |
| C | SER217 |
| C | LYS218 |
| C | LYS218 |
| C | GLY219 |
| C | ASN242 |
| C | ASN242 |
| C | LEU247 |
| C | HOH401 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for residue GLU C 302 |
| Chain | Residue |
| C | TYR61 |
| C | PRO89 |
| C | LEU90 |
| C | THR91 |
| C | ARG96 |
| C | GLY141 |
| C | SER142 |
| C | THR143 |
| C | GLU193 |
| C | HOH433 |
| C | HOH467 |
| C | HOH484 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 303 |
| Chain | Residue |
| C | HIS46 |
| C | HOH510 |
| C | HOH580 |
| C | HOH584 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue ZN C 304 |
| Chain | Residue |
| C | ASP156 |
| C | HOH415 |
| C | HOH578 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue ZN C 305 |
| Chain | Residue |
| C | HIS23 |
| C | GLU30 |
| C | ACT312 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 306 |
| Chain | Residue |
| C | GLU42 |
| C | HIS46 |
| C | LEU241 |
| C | HOH422 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue ZN C 307 |
| Chain | Residue |
| C | HOH407 |
| C | HOH458 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | binding site for residue ZN C 308 |
| Chain | Residue |
| C | ASP126 |
| C | HOH525 |
| site_id | AE5 |
| Number of Residues | 1 |
| Details | binding site for residue ZN C 309 |
| Chain | Residue |
| C | GLU132 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue ZN C 310 |
| Chain | Residue |
| C | HOH404 |
| C | HOH421 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue ACT C 311 |
| Chain | Residue |
| C | ARG180 |
| C | SER184 |
| C | LYS187 |
| site_id | AE8 |
| Number of Residues | 5 |
| Details | binding site for residue ACT C 312 |
| Chain | Residue |
| C | LYS20 |
| C | HIS23 |
| C | GLU30 |
| C | ZN305 |
| C | HOH480 |
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 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






