4FZ1
Crystal structure of acid-sensing ion channel in complex with psalmotoxin 1 at high pH
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005272 | molecular_function | sodium channel activity |
| A | 0006814 | biological_process | sodium ion transport |
| A | 0015280 | molecular_function | ligand-gated sodium channel activity |
| A | 0016020 | cellular_component | membrane |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0035821 | biological_process | modulation of process of another organism |
| D | 0090729 | molecular_function | toxin activity |
| D | 0099106 | molecular_function | ion channel regulator activity |
Functional Information from PROSITE/UniProt
| site_id | PS01206 |
| Number of Residues | 21 |
| Details | ASC Amiloride-sensitive sodium channels signature. YsiTaCridCeTryLVenCnC |
| Chain | Residue | Details |
| A | TYR304-CYS324 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"24507937","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4NTW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Motif: {"description":"GAS motif; ion selectivity filter","evidences":[{"source":"PubMed","id":"22842900","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24507937","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in channel desensitization; the process by which the channel becomes unresponsive to proton stimulation","evidences":[{"source":"PubMed","id":"22842900","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Involved in proton-dependent gating","evidences":[{"source":"UniProtKB","id":"P78348","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17882215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22760635","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22842900","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2QTS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Site: {"description":"Key residue for interaction with ASIC1a","evidences":[{"source":"PubMed","id":"22760635","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22842900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248594","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Site: {"description":"Key residue for interaction with ASIC1a","evidences":[{"source":"PubMed","id":"21825095","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22760635","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22842900","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
