5CBS
Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the antagonist (R)-2-amino-3-(3'-hydroxybiphenyl-3-yl)propanoic acid at 1.8A resolution
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 |
| D | 0015276 | molecular_function | ligand-gated monoatomic ion channel activity |
| D | 0016020 | cellular_component | membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue E42 A 301 |
| Chain | Residue |
| A | TYR58 |
| A | LYS215 |
| A | TYR217 |
| A | EDO304 |
| A | HOH450 |
| A | HOH541 |
| A | PRO86 |
| A | LEU87 |
| A | THR88 |
| A | ARG93 |
| A | ILE108 |
| A | SER139 |
| A | GLU190 |
| A | ASP213 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | LYS47 |
| A | ARG145 |
| A | TRP156 |
| A | ARG160 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 303 |
| Chain | Residue |
| A | MET16 |
| A | HIS20 |
| A | GLU21 |
| A | ARG28 |
| A | HOH425 |
| A | HOH474 |
| A | HOH624 |
| C | HIS43 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 304 |
| Chain | Residue |
| A | TYR58 |
| A | GLU190 |
| A | TYR217 |
| A | E42301 |
| A | HOH429 |
| A | HOH445 |
| A | HOH475 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 305 |
| Chain | Residue |
| A | PRO102 |
| A | PHE103 |
| A | MET104 |
| A | SER105 |
| A | ASN239 |
| A | HOH412 |
| A | HOH629 |
| C | SER214 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 306 |
| Chain | Residue |
| A | SER137 |
| A | GLY138 |
| A | HOH437 |
| A | HOH519 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 307 |
| Chain | Residue |
| A | LYS113 |
| A | HOH410 |
| D | LYS79 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 308 |
| Chain | Residue |
| A | GLU24 |
| A | GLY25 |
| A | ARG28 |
| A | LYS49 |
| A | HOH604 |
| A | HOH615 |
| C | GLN241 |
| site_id | AC9 |
| Number of Residues | 13 |
| Details | binding site for residue E42 B 301 |
| Chain | Residue |
| B | TYR58 |
| B | PRO86 |
| B | LEU87 |
| B | THR88 |
| B | ARG93 |
| B | ILE108 |
| B | SER139 |
| B | GLU190 |
| B | ASP213 |
| B | LYS215 |
| B | EDO304 |
| B | HOH422 |
| B | HOH557 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| B | HIS20 |
| B | GLU21 |
| B | ARG28 |
| B | HIS43 |
| B | HOH471 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 303 |
| Chain | Residue |
| B | ARG145 |
| B | TRP156 |
| B | ARG160 |
| D | LYS47 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| B | TYR58 |
| B | GLU190 |
| B | TYR217 |
| B | E42301 |
| B | HOH443 |
| B | HOH573 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| B | SER214 |
| B | HOH555 |
| D | PRO102 |
| D | SER105 |
| D | ASN239 |
| D | EDO307 |
| D | HOH425 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue EDO B 306 |
| Chain | Residue |
| B | PRO102 |
| B | PHE103 |
| B | MET104 |
| B | SER105 |
| B | HOH412 |
| B | HOH535 |
| B | HOH580 |
| D | SER214 |
| D | HOH401 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 307 |
| Chain | Residue |
| B | SER137 |
| B | GLY138 |
| B | HOH437 |
| B | HOH477 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 308 |
| Chain | Residue |
| B | SER105 |
| B | SER191 |
| B | GLU195 |
| B | ASN211 |
| B | HOH519 |
| B | HOH609 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 309 |
| Chain | Residue |
| B | GLU24 |
| B | GLY25 |
| B | ARG28 |
| B | LYS49 |
| B | HOH603 |
| D | ARG146 |
| D | LYS148 |
| D | HOH629 |
| site_id | AD9 |
| Number of Residues | 13 |
| Details | binding site for residue E42 C 301 |
| Chain | Residue |
| C | TYR58 |
| C | PRO86 |
| C | LEU87 |
| C | THR88 |
| C | ARG93 |
| C | LEU106 |
| C | ILE108 |
| C | SER139 |
| C | GLU190 |
| C | ASP213 |
| C | TYR217 |
| C | HOH424 |
| C | HOH443 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 302 |
| Chain | Residue |
| A | HIS43 |
| C | HIS20 |
| C | GLU21 |
| C | ARG28 |
| C | GOL305 |
| C | HOH434 |
| site_id | AE2 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 C 303 |
| Chain | Residue |
| C | SER105 |
| C | SER191 |
| C | GLU195 |
| C | ASN211 |
| C | LYS248 |
| C | HOH478 |
| C | HOH629 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 304 |
| Chain | Residue |
| C | ARG145 |
| C | TRP156 |
| C | ARG160 |
| site_id | AE4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL C 305 |
| Chain | Residue |
| A | HIS43 |
| A | LYS237 |
| A | GLN241 |
| C | LEU23 |
| C | ARG28 |
| C | SO4302 |
| C | HOH434 |
| C | HOH594 |
| site_id | AE5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 306 |
| Chain | Residue |
| C | LYS17 |
| C | ASN26 |
| C | GLU27 |
| C | TYR29 |
| C | GLU30 |
| C | VAL34 |
| C | HOH429 |
| C | HOH439 |
| C | HOH445 |
| site_id | AE6 |
| Number of Residues | 3 |
| Details | binding site for residue CL C 307 |
| Chain | Residue |
| C | SER137 |
| C | GLY138 |
| C | HOH627 |
| site_id | AE7 |
| Number of Residues | 14 |
| Details | binding site for residue E42 D 301 |
| Chain | Residue |
| D | TYR58 |
| D | PRO86 |
| D | LEU87 |
| D | THR88 |
| D | ARG93 |
| D | ILE108 |
| D | SER139 |
| D | GLU190 |
| D | ASP213 |
| D | LYS215 |
| D | TYR217 |
| D | EDO305 |
| D | HOH411 |
| D | HOH547 |
| site_id | AE8 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 D 302 |
| Chain | Residue |
| D | SER105 |
| D | SER191 |
| D | GLU195 |
| D | ASN211 |
| D | HOH492 |
| site_id | AE9 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 303 |
| Chain | Residue |
| D | HIS20 |
| D | GLU21 |
| D | ARG28 |
| D | HIS43 |
| D | HOH466 |
| D | HOH476 |
| D | HOH561 |
| site_id | AF1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 304 |
| Chain | Residue |
| D | ARG145 |
| D | TRP156 |
| D | ARG160 |
| D | HOH552 |
| site_id | AF2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 305 |
| Chain | Residue |
| D | TYR58 |
| D | GLU190 |
| D | MET193 |
| D | TYR217 |
| D | E42301 |
| D | HOH416 |
| D | HOH555 |
| site_id | AF3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 306 |
| Chain | Residue |
| D | SER137 |
| D | GLY138 |
| D | HOH464 |
| D | HOH572 |
| site_id | AF4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 307 |
| Chain | Residue |
| B | EDO305 |
| D | MET104 |
| D | SER105 |
| D | ASP245 |
| D | HOH402 |
| D | HOH407 |
| D | HOH425 |
| site_id | AF5 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 308 |
| Chain | Residue |
| D | MET15 |
| D | MET16 |
| D | HOH405 |
| D | HOH460 |
| site_id | AF6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO D 309 |
| Chain | Residue |
| D | ASN249 |
| D | ASP254 |
| D | HOH414 |
| D | HOH627 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| 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 | 12 |
| 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 | 4 |
| 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 | 4 |
| 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 | 4 |
| 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 | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






