7LG1
Cryo-EM structure of human cGMP-bound CNGA1_E365Q channel in Na+/Ca2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005216 | molecular_function | monoatomic ion channel activity |
| A | 0005221 | molecular_function | intracellularly cyclic nucleotide-activated monoatomic cation channel activity |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0016020 | cellular_component | membrane |
| A | 0055085 | biological_process | transmembrane transport |
| B | 0005216 | molecular_function | monoatomic ion channel activity |
| B | 0005221 | molecular_function | intracellularly cyclic nucleotide-activated monoatomic cation channel activity |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0016020 | cellular_component | membrane |
| B | 0055085 | biological_process | transmembrane transport |
| C | 0005216 | molecular_function | monoatomic ion channel activity |
| C | 0005221 | molecular_function | intracellularly cyclic nucleotide-activated monoatomic cation channel activity |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0016020 | cellular_component | membrane |
| C | 0055085 | biological_process | transmembrane transport |
| D | 0005216 | molecular_function | monoatomic ion channel activity |
| D | 0005221 | molecular_function | intracellularly cyclic nucleotide-activated monoatomic cation channel activity |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0016020 | cellular_component | membrane |
| D | 0055085 | biological_process | transmembrane transport |
Functional Information from PROSITE/UniProt
| site_id | PS00888 |
| Number of Residues | 17 |
| Details | CNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. ICkKGDiGReMYIIkeG |
| Chain | Residue | Details |
| A | ILE506-GLY522 |
| site_id | PS00889 |
| Number of Residues | 24 |
| Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEiSIlnikgskagnrRTAnIkS |
| Chain | Residue | Details |
| A | PHE544-SER567 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 84 |
| Details | TRANSMEM: Helical; Name=S1 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| A | TYR166-ALA187 | |
| B | TYR166-ALA187 | |
| C | TYR166-ALA187 | |
| D | TYR166-ALA187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 140 |
| Details | TOPO_DOM: Extracellular => ECO:0000305 |
| Chain | Residue | Details |
| A | CYS188-LEU197 | |
| D | CYS188-LEU197 | |
| D | LEU263-TYR267 | |
| D | PHE318-PRO340 | |
| A | LEU263-TYR267 | |
| A | PHE318-PRO340 | |
| B | CYS188-LEU197 | |
| B | LEU263-TYR267 | |
| B | PHE318-PRO340 | |
| C | CYS188-LEU197 | |
| C | LEU263-TYR267 | |
| C | PHE318-PRO340 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | TRANSMEM: Helical; Name=S2 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| A | GLU198-ARG218 | |
| B | GLU198-ARG218 | |
| C | GLU198-ARG218 | |
| D | GLU198-ARG218 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1260 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| A | THR219-ASN243 | |
| D | THR219-ASN243 | |
| D | ARG287-ASN293 | |
| D | SER401-PRO686 | |
| A | ARG287-ASN293 | |
| A | SER401-PRO686 | |
| B | THR219-ASN243 | |
| B | ARG287-ASN293 | |
| B | SER401-PRO686 | |
| C | THR219-ASN243 | |
| C | ARG287-ASN293 | |
| C | SER401-PRO686 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 72 |
| Details | TRANSMEM: Helical; Name=S3 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| A | LEU244-LYS262 | |
| B | LEU244-LYS262 | |
| C | LEU244-LYS262 | |
| D | LEU244-LYS262 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 72 |
| Details | TRANSMEM: Helical; Name=S4 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| A | PRO268-GLN286 | |
| B | PRO268-GLN286 | |
| C | PRO268-GLN286 | |
| D | PRO268-GLN286 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 92 |
| Details | TRANSMEM: Helical; Name=S5 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| A | TYR294-VAL317 | |
| B | TYR294-VAL317 | |
| C | TYR294-VAL317 | |
| D | TYR294-VAL317 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 136 |
| Details | TRANSMEM: Helical; Name=P-helix => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| A | GLU341-TYR375 | |
| B | GLU341-TYR375 | |
| C | GLU341-TYR375 | |
| D | GLU341-TYR375 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 96 |
| Details | TRANSMEM: Helical; Name=S6 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| A | VAL376-ILE400 | |
| B | VAL376-ILE400 | |
| C | VAL376-ILE400 | |
| D | VAL376-ILE400 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RHH |
| Chain | Residue | Details |
| A | GLY541 | |
| C | PHE544 | |
| C | ALA557 | |
| C | GLY558 | |
| D | GLY541 | |
| D | PHE544 | |
| D | ALA557 | |
| D | GLY558 | |
| A | PHE544 | |
| A | ALA557 | |
| A | GLY558 | |
| B | GLY541 | |
| B | PHE544 | |
| B | ALA557 | |
| B | GLY558 | |
| C | GLY541 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | SITE: Central gate => ECO:0000305|PubMed:34699778 |
| Chain | Residue | Details |
| A | GLY385 | |
| A | PHE389 | |
| B | GLY385 | |
| B | PHE389 | |
| C | GLY385 | |
| C | PHE389 | |
| D | GLY385 | |
| D | PHE389 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000250|UniProtKB:Q00194 |
| Chain | Residue | Details |
| A | ILE325 | |
| B | ILE325 | |
| C | ILE325 | |
| D | ILE325 |
