7RHK
Cryo-EM structure of human rod CNGA1/B1 channel in L-cis-Diltiazem-trapped closed state
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 | 0005221 | molecular_function | intracellularly cyclic nucleotide-activated monoatomic cation channel activity |
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. VCkKGEiGReMYIIqaG |
Chain | Residue | Details |
B | VAL989-GLY1005 | |
C | 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 | |
C | 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 | |
A | 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 | |
A | CYS188-LEU197 | |
A | LEU263-TYR267 | |
A | 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 | |
A | 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 | |
A | THR219-ASN243 | |
A | ARG287-ASN293 | |
A | 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 | |
A | 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 | |
A | 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 | |
A | 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 | |
A | 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 | |
A | 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 | |
C | GLY558 | |
A | GLY541 | |
A | PHE544 | |
A | ALA557 | |
A | 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 | |
C | PHE389 | |
A | GLY385 | |
A | 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 | |
A | 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 |