4D01
Crystal Structure of the Extracellular Domain of the Human Alpha9 Nicotinic Acetylcholine Receptor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004888 | molecular_function | transmembrane signaling receptor activity |
| A | 0005216 | molecular_function | monoatomic ion channel activity |
| A | 0005230 | molecular_function | extracellular ligand-gated monoatomic ion channel activity |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0016020 | cellular_component | membrane |
| A | 0022848 | molecular_function | acetylcholine-gated monoatomic cation-selective channel activity |
| A | 0034220 | biological_process | monoatomic ion transmembrane transport |
| A | 0045211 | cellular_component | postsynaptic membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00236 |
| Number of Residues | 15 |
| Details | NEUROTR_ION_CHANNEL Neurotransmitter-gated ion-channels signature. CvVdVtyFPfDnqqC |
| Chain | Residue | Details |
| A | CYS130-CYS144 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"25282151","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UXU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Site: {"description":"Key residue important for potent inhibition of the CHRNA9:CHRNA10 receptor by the alpha-conotoxin RgIA (AC P0C1D0)","evidences":[{"source":"UniProtKB","id":"P43144","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"25282151","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4D01","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UXU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UY2","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
