5ZG3
Crystal structure of the GluA2o LBD in complex with glutamate and TAK-137
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 |
| E | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| E | 0016020 | cellular_component | membrane |
| F | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| F | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue 9C6 A 1001 |
| Chain | Residue |
| A | ILE502 |
| B | LYS751 |
| B | ASN775 |
| A | PRO515 |
| A | PHE516 |
| A | SER750 |
| A | LYS751 |
| A | GLY752 |
| B | LYS514 |
| B | PRO515 |
| B | SER750 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue GLU A 1002 |
| Chain | Residue |
| A | TYR471 |
| A | PRO499 |
| A | LEU500 |
| A | THR501 |
| A | ARG506 |
| A | LEU671 |
| A | GLY674 |
| A | SER675 |
| A | THR676 |
| A | GLU726 |
| A | TYR753 |
| A | HOH1116 |
| A | HOH1134 |
| A | HOH1148 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue GLU B 901 |
| Chain | Residue |
| B | TYR471 |
| B | PRO499 |
| B | LEU500 |
| B | THR501 |
| B | ARG506 |
| B | GLY674 |
| B | SER675 |
| B | THR676 |
| B | GLU726 |
| B | TYR753 |
| B | HOH1006 |
| B | HOH1014 |
| B | HOH1027 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 902 |
| Chain | Residue |
| B | GLU452 |
| B | LYS455 |
| B | HIS456 |
| B | GLN777 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 903 |
| Chain | Residue |
| B | GLU443 |
| B | LYS786 |
| B | HOH1060 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 904 |
| Chain | Residue |
| B | ALA473 |
| B | ASP475 |
| B | ASN482 |
| B | SER673 |
| B | HOH1040 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 905 |
| Chain | Residue |
| B | HIS456 |
| B | HOH1154 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 801 |
| Chain | Residue |
| A | GLU452 |
| A | HIS456 |
| C | GLU699 |
| C | HOH1085 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue GLU C 802 |
| Chain | Residue |
| C | TYR471 |
| C | PRO499 |
| C | LEU500 |
| C | THR501 |
| C | ARG506 |
| C | LEU671 |
| C | GLY674 |
| C | SER675 |
| C | THR676 |
| C | GLU726 |
| C | TYR753 |
| C | HOH935 |
| C | HOH956 |
| C | HOH958 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 803 |
| Chain | Residue |
| C | GLU452 |
| C | HIS456 |
| C | LEU774 |
| C | HOH1082 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue ACT C 804 |
| Chain | Residue |
| C | ARG713 |
| C | SER717 |
| C | LYS720 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue ACT C 805 |
| Chain | Residue |
| C | ASP781 |
| C | HOH1063 |
| D | ASN747 |
| D | ASP749 |
| D | SER750 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue ACT C 806 |
| Chain | Residue |
| C | ASN747 |
| C | LEU748 |
| C | ASP749 |
| C | SER750 |
| C | HOH1078 |
| D | ASP781 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue ZN D 801 |
| Chain | Residue |
| D | ASP689 |
| site_id | AD6 |
| Number of Residues | 24 |
| Details | binding site for residue 9C6 D 802 |
| Chain | Residue |
| C | HOH1077 |
| D | ILE502 |
| D | PRO515 |
| D | PHE516 |
| D | MET517 |
| D | SER518 |
| D | SER750 |
| D | LYS751 |
| D | GLY752 |
| D | ASN775 |
| D | HOH901 |
| D | HOH902 |
| D | HOH1048 |
| D | HOH1073 |
| C | ILE502 |
| C | PRO515 |
| C | PHE516 |
| C | MET517 |
| C | SER518 |
| C | SER750 |
| C | LYS751 |
| C | GLY752 |
| C | ASN775 |
| C | HOH1053 |
| site_id | AD7 |
| Number of Residues | 14 |
| Details | binding site for residue GLU D 803 |
| Chain | Residue |
| D | TYR471 |
| D | PRO499 |
| D | LEU500 |
| D | THR501 |
| D | ARG506 |
| D | LEU671 |
| D | GLY674 |
| D | SER675 |
| D | THR676 |
| D | GLU726 |
| D | TYR753 |
| D | HOH934 |
| D | HOH979 |
| D | HOH983 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue ZN D 804 |
| Chain | Residue |
| D | HIS433 |
| D | GLU440 |
| D | ACT807 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue ZN D 805 |
| Chain | Residue |
| D | GLU452 |
| D | HIS456 |
| D | HOH1083 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue ACT D 806 |
| Chain | Residue |
| D | ARG713 |
| D | LYS720 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue ACT D 807 |
| Chain | Residue |
| D | LYS430 |
| D | HIS433 |
| D | GLU440 |
| D | ZN804 |
| D | HOH908 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 808 |
| Chain | Residue |
| D | GLU699 |
| D | HOH1078 |
| E | GLU452 |
| E | HIS456 |
| site_id | AE4 |
| Number of Residues | 11 |
| Details | binding site for residue 9C6 E 1001 |
| Chain | Residue |
| E | ILE502 |
| E | PRO515 |
| E | PHE516 |
| E | SER750 |
| E | LYS751 |
| E | GLY752 |
| F | LYS514 |
| F | PRO515 |
| F | SER750 |
| F | LYS751 |
| F | ASN775 |
| site_id | AE5 |
| Number of Residues | 14 |
| Details | binding site for residue GLU E 1002 |
| Chain | Residue |
| E | TYR471 |
| E | PRO499 |
| E | LEU500 |
| E | THR501 |
| E | ARG506 |
| E | LEU671 |
| E | GLY674 |
| E | SER675 |
| E | THR676 |
| E | GLU726 |
| E | TYR753 |
| E | HOH1106 |
| E | HOH1142 |
| E | HOH1154 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue ZN E 1003 |
| Chain | Residue |
| E | HIS433 |
| E | ACT1004 |
| site_id | AE7 |
| Number of Residues | 3 |
| Details | binding site for residue ACT E 1004 |
| Chain | Residue |
| E | MET429 |
| E | HIS433 |
| E | ZN1003 |
| site_id | AE8 |
| Number of Residues | 2 |
| Details | binding site for residue ZN F 801 |
| Chain | Residue |
| F | HIS433 |
| F | ACT806 |
| site_id | AE9 |
| Number of Residues | 13 |
| Details | binding site for residue GLU F 802 |
| Chain | Residue |
| F | TYR471 |
| F | PRO499 |
| F | LEU500 |
| F | THR501 |
| F | ARG506 |
| F | GLY674 |
| F | SER675 |
| F | THR676 |
| F | GLU726 |
| F | TYR753 |
| F | HOH907 |
| F | HOH915 |
| F | HOH917 |
| site_id | AF1 |
| Number of Residues | 2 |
| Details | binding site for residue ZN F 803 |
| Chain | Residue |
| F | GLU452 |
| F | HIS456 |
| site_id | AF2 |
| Number of Residues | 2 |
| Details | binding site for residue ZN F 804 |
| Chain | Residue |
| F | ASP475 |
| F | ACT805 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue ACT F 805 |
| Chain | Residue |
| F | ASP475 |
| F | ASP477 |
| F | THR478 |
| F | ZN804 |
| site_id | AF4 |
| Number of Residues | 3 |
| Details | binding site for residue ACT F 806 |
| Chain | Residue |
| F | HIS433 |
| F | GLU434 |
| F | ZN801 |
| site_id | AF5 |
| Number of Residues | 5 |
| Details | binding site for residue ACT F 807 |
| Chain | Residue |
| F | ALA473 |
| F | ARG474 |
| F | ASP475 |
| F | ASN482 |
| F | SER673 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20614889","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XHD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20614889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21531559","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XHD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3R7X","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20614889","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21531559","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2XHD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"UniProtKB","id":"P19491","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by PKG","evidences":[{"source":"UniProtKB","id":"P19491","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






