7RHI
Cryo-EM structure of human rod CNGA1/B1 channel in cGMP-bound openII state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005216 | molecular_function | monoatomic ion channel activity |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0016020 | cellular_component | membrane |
| A | 0055085 | biological_process | transmembrane transport |
| C | 0005216 | molecular_function | monoatomic ion 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 | 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. VCkKGEiGReMYIIqaG |
| Chain | Residue | Details |
| B | VAL989-GLY1005 | |
| A | ILE506-GLY522 |
| site_id | PS00889 |
| Number of Residues | 21 |
| Details | CNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEiSLlavgggnr...RTAnVvA |
| Chain | Residue | Details |
| B | PHE1028-ALA1048 | |
| A | PHE544-SER567 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=S1 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| B | VAL657-TRP678 | |
| C | TYR166-ALA187 | |
| D | TYR166-ALA187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 45 |
| Details | TOPO_DOM: Extracellular => ECO:0000305 |
| Chain | Residue | Details |
| B | ALA679-ASN687 | |
| B | LEU745-LEU760 | |
| B | TYR809-SER831 | |
| C | CYS188-LEU197 | |
| C | LEU263-TYR267 | |
| C | PHE318-PRO340 | |
| D | CYS188-LEU197 | |
| D | LEU263-TYR267 | |
| D | PHE318-PRO340 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 21 |
| Details | TRANSMEM: Helical; Name=S2 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| B | ILE688-PHE709 | |
| C | GLU198-ARG218 | |
| D | GLU198-ARG218 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 391 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
| Chain | Residue | Details |
| B | GLN710-ASP724 | |
| B | GLU774-LYS785 | |
| B | ALA885-GLU1251 | |
| C | THR219-ASN243 | |
| C | ARG287-ASN293 | |
| C | SER401-PRO686 | |
| D | THR219-ASN243 | |
| D | ARG287-ASN293 | |
| D | SER401-PRO686 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 19 |
| Details | TRANSMEM: Helical; Name=S3 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| B | LYS725-SER744 | |
| C | LEU244-LYS262 | |
| D | LEU244-LYS262 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | TRANSMEM: Helical; Name=S4 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| B | LEU761-PHE773 | |
| C | PRO268-GLN286 | |
| D | PRO268-GLN286 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | TRANSMEM: Helical; Name=S5 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| B | ALA786-LEU808 | |
| C | TYR294-VAL317 | |
| D | TYR294-VAL317 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 26 |
| Details | TRANSMEM: Helical; Name=P-helix => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| B | TYR832-ILE858 | |
| C | GLU341-TYR375 | |
| D | GLU341-TYR375 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 25 |
| Details | TRANSMEM: Helical; Name=S6 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9 |
| Chain | Residue | Details |
| B | VAL859-GLY884 | |
| C | VAL376-ILE400 | |
| D | VAL376-ILE400 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RHI |
| Chain | Residue | Details |
| B | GLY1029 | |
| D | PHE544 | |
| D | ALA557 | |
| D | GLY558 | |
| B | GLU1030 | |
| B | SER1032 | |
| A | GLY558 | |
| C | GLY541 | |
| C | PHE544 | |
| C | ALA557 | |
| C | GLY558 | |
| D | GLY541 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RHH |
| Chain | Residue | Details |
| B | ARG1042 | |
| A | PHE389 | |
| C | GLY385 | |
| C | PHE389 | |
| D | GLY385 | |
| D | PHE389 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RHH, ECO:0007744|PDB:7RHI |
| Chain | Residue | Details |
| B | THR1043 | |
| C | ILE325 | |
| D | ILE325 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | SITE: Central gate => ECO:0000305|PubMed:34699778 |
| Chain | Residue | Details |
| B | PHE872 | |
| B | ILE876 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | SITE: Occludes the pore below the central gate => ECO:0000305|PubMed:34699778 |
| Chain | Residue | Details |
| B | ARG880 |
