3C34
Crystal structure of GluR5 ligand-binding core in complex with rubidium at 1.82 Angstrom resolution
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE RB B 301 |
| Chain | Residue |
| B | GLU96 |
| B | ILE99 |
| B | ASP100 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE RB A 302 |
| Chain | Residue |
| A | GLU96 |
| A | ILE99 |
| A | ASP100 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE RB A 303 |
| Chain | Residue |
| A | SER22 |
| B | LEU181 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE RB A 304 |
| Chain | Residue |
| B | SER22 |
| A | LEU181 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE RB A 305 |
| Chain | Residue |
| A | LYS150 |
| A | GLU155 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE RB B 306 |
| Chain | Residue |
| B | THR118 |
| B | ILE120 |
| B | ASP121 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 307 |
| Chain | Residue |
| A | LYS103 |
| A | ARG227 |
| B | LYS103 |
| B | ARG227 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 308 |
| Chain | Residue |
| A | ARG31 |
| A | LYS54 |
| A | LEU55 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 309 |
| Chain | Residue |
| B | ARG31 |
| B | LYS54 |
| B | LEU55 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 310 |
| Chain | Residue |
| B | ARG20 |
| B | SER22 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE KAI A 401 |
| Chain | Residue |
| A | GLU13 |
| A | TYR61 |
| A | PRO88 |
| A | THR90 |
| A | ARG95 |
| A | GLY140 |
| A | SER141 |
| A | THR142 |
| A | GLU190 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE KAI B 401 |
| Chain | Residue |
| B | GLU13 |
| B | TYR61 |
| B | PRO88 |
| B | THR90 |
| B | ARG95 |
| B | GLY140 |
| B | SER141 |
| B | THR142 |
| B | GLU190 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 402 |
| Chain | Residue |
| B | LYS60 |
| B | TYR61 |
| B | GLY62 |
| B | ALA63 |
| B | ARG138 |
| B | ASP139 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 402 |
| Chain | Residue |
| A | LYS60 |
| A | TYR61 |
| A | GLY62 |
| A | ALA63 |
| A | ARG138 |
| A | ASP139 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 403 |
| Chain | Residue |
| A | LYS54 |
| A | LEU55 |
| A | PRO57 |
| B | SER167 |
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 | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
