5H8S
Structure of the human GluA2 LBD in complex with GNE3419
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 | HOH428 |
| A | HOH444 |
| A | HOH466 |
| A | PRO89 |
| A | LEU90 |
| A | THR91 |
| A | ARG96 |
| A | GLY141 |
| A | SER142 |
| A | THR143 |
| A | GLU193 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | binding site for residue 5YC A 302 |
| Chain | Residue |
| A | PRO105 |
| A | MET107 |
| A | SER108 |
| A | SER217 |
| A | LYS218 |
| A | GLY219 |
| A | SER242 |
| A | HOH494 |
| A | HOH528 |
| B | ILE92 |
| B | PRO105 |
| B | MET107 |
| B | SER108 |
| B | SER217 |
| B | LYS218 |
| B | GLY219 |
| B | HOH454 |
| B | HOH477 |
| B | HOH490 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 303 |
| Chain | Residue |
| A | GLU42 |
| A | HIS46 |
| A | CAC305 |
| C | GLU166 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 304 |
| Chain | Residue |
| A | HIS23 |
| A | HOH579 |
| B | ASP65 |
| B | HOH526 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue CAC A 305 |
| Chain | Residue |
| A | GLU42 |
| A | HIS46 |
| A | ZN303 |
| A | HOH401 |
| C | ARG163 |
| C | ALA165 |
| C | GLU166 |
| C | SER168 |
| C | PHE170 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue GLU C 301 |
| Chain | Residue |
| C | TYR61 |
| C | PRO89 |
| C | LEU90 |
| C | THR91 |
| C | ARG96 |
| C | GLY141 |
| C | SER142 |
| C | THR143 |
| C | GLU193 |
| C | TYR220 |
| C | HOH469 |
| C | HOH504 |
| C | HOH509 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | binding site for residue 5YC C 302 |
| Chain | Residue |
| C | ILE92 |
| C | ILE92 |
| C | PRO105 |
| C | PRO105 |
| C | MET107 |
| C | MET107 |
| C | SER108 |
| C | SER108 |
| C | SER217 |
| C | SER217 |
| C | LYS218 |
| C | LYS218 |
| C | GLY219 |
| C | GLY219 |
| C | HOH419 |
| C | HOH419 |
| C | HOH496 |
| C | HOH496 |
| C | HOH549 |
| C | HOH549 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 303 |
| Chain | Residue |
| B | HIS23 |
| C | HIS23 |
| C | GLU30 |
| C | HOH618 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 304 |
| Chain | Residue |
| A | GLU166 |
| C | GLU42 |
| C | HIS46 |
| C | LEU241 |
| C | HOH607 |
| site_id | AD1 |
| Number of Residues | 14 |
| Details | binding site for residue GLU B 301 |
| Chain | Residue |
| B | GLU193 |
| B | TYR220 |
| B | HOH431 |
| B | HOH447 |
| B | HOH452 |
| B | TYR61 |
| B | PRO89 |
| B | LEU90 |
| B | THR91 |
| B | ARG96 |
| B | LEU138 |
| B | GLY141 |
| B | SER142 |
| B | THR143 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 302 |
| Chain | Residue |
| B | GLU42 |
| B | LYS45 |
| B | HIS46 |
| B | HOH488 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue ZN B 303 |
| Chain | Residue |
| B | ASP156 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| 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 | 3 |
| 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 | 3 |
| 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 | 3 |
| 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 | 3 |
| 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 | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
