4NTY
Cesium sites in the crystal structure of acid-sensing ion channel in complex with snake toxin
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 |
B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
B | 0005576 | cellular_component | extracellular region |
B | 0010466 | biological_process | negative regulation of peptidase activity |
B | 0035821 | biological_process | modulation of process of another organism |
B | 0090729 | molecular_function | toxin activity |
B | 0099106 | molecular_function | ion channel regulator activity |
C | 0004623 | molecular_function | phospholipase A2 activity |
C | 0005509 | molecular_function | calcium ion binding |
C | 0005543 | molecular_function | phospholipid binding |
C | 0005576 | cellular_component | extracellular region |
C | 0006644 | biological_process | phospholipid metabolic process |
C | 0016042 | biological_process | lipid catabolic process |
C | 0016787 | molecular_function | hydrolase activity |
C | 0035821 | biological_process | modulation of process of another organism |
C | 0047498 | molecular_function | calcium-dependent phospholipase A2 activity |
C | 0050482 | biological_process | arachidonic acid secretion |
C | 0090729 | molecular_function | toxin activity |
C | 0099106 | molecular_function | ion channel regulator activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CS A 501 |
Chain | Residue |
A | TYR68 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CS A 503 |
Chain | Residue |
A | THR295 |
A | GLU299 |
A | TYR301 |
A | ASP302 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CS A 504 |
Chain | Residue |
A | ASP238 |
A | THR240 |
A | PE4513 |
A | HOH657 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS A 505 |
Chain | Residue |
A | TYR110 |
A | HIS111 |
A | TYR123 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS A 506 |
Chain | Residue |
A | LEU375 |
A | LEU375 |
A | LEU375 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CS A 507 |
Chain | Residue |
A | LYS373 |
A | LYS373 |
A | LYS373 |
A | HOH654 |
A | HOH654 |
A | HOH654 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CS A 508 |
Chain | Residue |
A | VAL319 |
A | GLU320 |
A | ASN323 |
C | ASN3 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CS A 510 |
Chain | Residue |
A | GLU183 |
A | PHE185 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 512 |
Chain | Residue |
A | LYS212 |
A | ARG310 |
A | HOH604 |
site_id | BC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE PE4 A 513 |
Chain | Residue |
A | LEU96 |
A | GLU98 |
A | ARG191 |
A | ASP238 |
A | ASP350 |
A | GLU354 |
A | CS504 |
A | HOH667 |
A | HOH668 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CS B 101 |
Chain | Residue |
B | GLN45 |
B | HIS47 |
B | PHE48 |
B | HOH203 |
site_id | BC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CS B 102 |
Chain | Residue |
C | ASP31 |
C | SER32 |
site_id | BC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CS C 201 |
Chain | Residue |
B | SER29 |
C | PHE68 |
C | HOH304 |
site_id | BC5 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CS C 202 |
Chain | Residue |
C | SER80 |
C | ASN82 |
Functional Information from PROSITE/UniProt
site_id | PS00092 |
Number of Residues | 7 |
Details | N6_MTASE N-6 Adenine-specific DNA methylases signature. CYEDPPF |
Chain | Residue | Details |
B | CYS7-PHE13 |
site_id | PS00119 |
Number of Residues | 11 |
Details | PA2_ASP Phospholipase A2 aspartic acid active site. VCNCDRTAtLC |
Chain | Residue | Details |
C | VAL90-CYS100 |
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 | 1 |
Details | MOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:22094702 |
Chain | Residue | Details |
B | PCA1 |
site_id | SWS_FT_FI2 |
Number of Residues | 355 |
Details | TOPO_DOM: Extracellular |
Chain | Residue | Details |
A | LEU71-GLU426 |
site_id | SWS_FT_FI3 |
Number of Residues | 26 |
Details | TRANSMEM: Discontinuously helical |
Chain | Residue | Details |
A | VAL427-PHE453 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Important for channel gating |
Chain | Residue | Details |
A | TYR72 | |
A | TRP288 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Important for channel desensitizing |
Chain | Residue | Details |
A | GLU80 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:17882215, ECO:0000269|PubMed:22760635, ECO:0000269|PubMed:22842900 |
Chain | Residue | Details |
A | ASN367 | |
A | ASN394 |