5MFV
Crystal structure of the GluK1 ligand-binding domain in complex with kainate and BPAM-521 at 2.18 A resolution
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue 5PX A 901 |
| Chain | Residue |
| A | LYS531 |
| B | ILE519 |
| B | PRO532 |
| B | THR535 |
| B | LYS762 |
| B | GLY763 |
| A | PRO532 |
| A | PHE533 |
| A | MET534 |
| A | THR535 |
| A | LEU783 |
| A | GLN786 |
| A | LEU791 |
| A | HOH1001 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue 5PX A 902 |
| Chain | Residue |
| A | ILE519 |
| A | PRO532 |
| A | THR535 |
| A | SER761 |
| A | LYS762 |
| A | GLY763 |
| B | LYS531 |
| B | PRO532 |
| B | PHE533 |
| B | MET534 |
| B | LEU783 |
| B | GLN786 |
| B | LEU791 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue KAI A 903 |
| Chain | Residue |
| A | GLU441 |
| A | TYR489 |
| A | PRO516 |
| A | THR518 |
| A | ARG523 |
| A | GLY688 |
| A | SER689 |
| A | THR690 |
| A | SER721 |
| A | GLU738 |
| A | HOH1036 |
| A | HOH1048 |
| A | HOH1057 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 904 |
| Chain | Residue |
| A | LYS531 |
| B | LYS531 |
| B | HOH1070 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 A 905 |
| Chain | Residue |
| A | GLN786 |
| A | HIS792 |
| A | HOH1031 |
| B | ASP760 |
| B | SER761 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 906 |
| Chain | Residue |
| A | LYS488 |
| A | TYR489 |
| A | ARG686 |
| A | ASP687 |
| A | GLY688 |
| A | LYS719 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue KAI B 901 |
| Chain | Residue |
| B | GLU441 |
| B | TYR489 |
| B | PRO516 |
| B | THR518 |
| B | ARG523 |
| B | GLY688 |
| B | SER689 |
| B | THR690 |
| B | GLU738 |
| B | HOH1023 |
| B | HOH1043 |
| B | HOH1072 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 902 |
| Chain | Residue |
| A | ASP760 |
| A | SER761 |
| B | GLN786 |
| B | HIS792 |
| B | HOH1045 |
| B | HOH1079 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 903 |
| Chain | Residue |
| B | ARG459 |
| B | HOH1006 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue ACT B 904 |
| Chain | Residue |
| B | ARG448 |
| B | SER450 |
| B | LYS452 |
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 |
