6FAZ
Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the positive allosteric modulator TDPAM01 at 1.4 A resolution.
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | SER140 |
| A | LYS144 |
| A | ARG148 |
| A | HOH434 |
| A | HOH467 |
| A | HOH489 |
| A | HOH603 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | HOH420 |
| A | HOH506 |
| A | LYS82 |
| A | LYS116 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | GLU97 |
| A | ASP101 |
| A | PHE102 |
| A | HOH433 |
| A | HOH574 |
| A | HOH649 |
| B | LYS104 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 304 |
| Chain | Residue |
| A | GLY28 |
| A | ARG31 |
| A | LYS52 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 305 |
| Chain | Residue |
| A | GLU33 |
| A | LYS253 |
| A | TRP254 |
| A | LYS258 |
| A | HOH549 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 306 |
| Chain | Residue |
| A | ARG148 |
| A | TRP159 |
| A | ARG163 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 307 |
| Chain | Residue |
| A | HIS46 |
| A | LYS240 |
| A | GLN244 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 308 |
| Chain | Residue |
| A | SER194 |
| A | GLU198 |
| A | LYS210 |
| A | ASN214 |
| A | HOH595 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 309 |
| Chain | Residue |
| A | LEU78 |
| A | VAL79 |
| A | GLY81 |
| A | LYS117 |
| A | MET209 |
| A | PRO225 |
| A | LYS226 |
| A | HOH401 |
| A | HOH403 |
| A | HOH481 |
| A | HOH632 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue CL A 310 |
| Chain | Residue |
| A | LYS4 |
| A | THR5 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue ACT A 311 |
| Chain | Residue |
| A | ILE152 |
| A | ALA153 |
| A | HOH439 |
| A | HOH619 |
| site_id | AD3 |
| Number of Residues | 13 |
| Details | binding site for residue GLU A 312 |
| Chain | Residue |
| A | TYR61 |
| A | PRO89 |
| A | LEU90 |
| A | THR91 |
| A | ARG96 |
| A | GLY141 |
| A | SER142 |
| A | THR143 |
| A | GLU193 |
| A | TYR220 |
| A | HOH432 |
| A | HOH468 |
| A | HOH488 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 313 |
| Chain | Residue |
| A | ASN214 |
| A | ASP216 |
| A | SER217 |
| B | ASP248 |
| site_id | AD5 |
| Number of Residues | 14 |
| Details | binding site for residue D45 B 301 |
| Chain | Residue |
| A | LYS104 |
| A | PRO105 |
| A | SER108 |
| A | SER217 |
| A | LYS218 |
| A | GLY219 |
| A | ASN242 |
| B | LYS104 |
| B | PRO105 |
| B | SER108 |
| B | LYS218 |
| B | GLY219 |
| B | ASN242 |
| B | HOH524 |
| site_id | AD6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| B | SER140 |
| B | LYS144 |
| B | ARG148 |
| B | HOH423 |
| B | HOH435 |
| B | HOH547 |
| B | HOH570 |
| site_id | AD7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| B | ARG31 |
| B | HOH425 |
| B | HOH460 |
| B | HOH482 |
| B | HOH494 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | ARG163 |
| B | HOH598 |
| B | ARG148 |
| B | TRP159 |
| site_id | AD9 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 305 |
| Chain | Residue |
| B | ASN22 |
| B | GLU24 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 306 |
| Chain | Residue |
| B | HIS46 |
| B | GLN244 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 307 |
| Chain | Residue |
| B | LYS50 |
| B | TYR51 |
| B | HOH589 |
| site_id | AE3 |
| Number of Residues | 1 |
| Details | binding site for residue CL B 308 |
| Chain | Residue |
| B | ALA153 |
| site_id | AE4 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 309 |
| Chain | Residue |
| A | ASP248 |
| B | ASN214 |
| B | LEU215 |
| B | ASP216 |
| B | SER217 |
| B | HOH587 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue ACT B 310 |
| Chain | Residue |
| A | LYS104 |
| A | HOH694 |
| B | GLU97 |
| B | ASP101 |
| B | PHE102 |
| B | HOH610 |
| site_id | AE6 |
| Number of Residues | 13 |
| Details | binding site for residue GLU B 311 |
| Chain | Residue |
| B | TYR61 |
| B | PRO89 |
| B | LEU90 |
| B | THR91 |
| B | ARG96 |
| B | GLY141 |
| B | SER142 |
| B | THR143 |
| B | GLU193 |
| B | TYR220 |
| B | HOH444 |
| B | HOH462 |
| B | HOH463 |
| site_id | AE7 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 312 |
| Chain | Residue |
| B | ALA134 |
| B | TYR161 |
| B | ALA165 |
| B | GLU166 |
| B | PRO167 |
| B | VAL169 |
| B | ARG180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| 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 | 6 |
| 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 | 2 |
| 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 | 2 |
| 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 | 2 |
| 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 |






