4YMB
Structure of the ligand-binding domain of GluK1 in complex with the antagonist CNG10111
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | binding site for residue 4E7 A 301 |
| Chain | Residue |
| A | GLU13 |
| A | SER193 |
| A | TYR216 |
| A | HOH457 |
| A | HOH461 |
| A | HOH474 |
| A | HOH482 |
| A | HOH560 |
| A | TYR61 |
| A | PRO88 |
| A | LEU89 |
| A | THR90 |
| A | ARG95 |
| A | THR142 |
| A | MET189 |
| A | GLU190 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ACT A 302 |
| Chain | Residue |
| A | GLU175 |
| A | HOH414 |
| B | LEU12 |
| B | VAL56 |
| B | GLY59 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 303 |
| Chain | Residue |
| A | GLY62 |
| A | ALA63 |
| A | ARG95 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL A 304 |
| Chain | Residue |
| A | LYS103 |
| A | HOH497 |
| B | LYS103 |
| B | HOH459 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 305 |
| Chain | Residue |
| A | LEU55 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue PEG A 306 |
| Chain | Residue |
| A | HIS80 |
| A | PRO225 |
| A | HOH516 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | binding site for residue 4E7 B 301 |
| Chain | Residue |
| B | GLU13 |
| B | TYR61 |
| B | PRO88 |
| B | LEU89 |
| B | THR90 |
| B | ARG95 |
| B | VAL137 |
| B | THR142 |
| B | MET189 |
| B | GLU190 |
| B | SER193 |
| B | TYR216 |
| B | HOH480 |
| B | HOH503 |
| B | HOH605 |
| B | HOH646 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue ACT B 302 |
| Chain | Residue |
| A | THR10 |
| A | ILE11 |
| A | LEU12 |
| A | LEU55 |
| A | VAL56 |
| A | GLY59 |
| B | GLU175 |
| B | HOH426 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ACT B 303 |
| Chain | Residue |
| B | PRO119 |
| B | ILE120 |
| B | ASP125 |
| B | LYS128 |
| B | GLN129 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 304 |
| Chain | Residue |
| A | ARG20 |
| A | SER22 |
| B | HOH442 |
| site_id | AD2 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 305 |
| Chain | Residue |
| B | ARG31 |
| B | LEU55 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 306 |
| Chain | Residue |
| A | LYS171 |
| A | ASN172 |
| B | HOH403 |
| B | HOH412 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15710405","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YCJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15710405","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15721240","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YCJ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
