7LFT
Cryo-EM structure of human Apo CNGA1 channel in K+/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 | Transmembrane: {"description":"Helical; Name=S1","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 140 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | Transmembrane: {"description":"Helical; Name=S2","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 120 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 72 |
| Details | Transmembrane: {"description":"Helical; Name=S3","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 72 |
| Details | Transmembrane: {"description":"Helical; Name=S4","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 92 |
| Details | Transmembrane: {"description":"Helical; Name=S5","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 136 |
| Details | Transmembrane: {"description":"Helical; Name=P-helix","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 96 |
| Details | Transmembrane: {"description":"Helical; Name=S6","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 432 |
| Details | Region: {"description":"Ion conduction pathway","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 12 |
| Details | Region: {"description":"Selectivity filter","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 304 |
| Details | Region: {"description":"C-linker","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 480 |
| Details | Region: {"description":"Cyclic nucleotide-binding domain","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7RHI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RHH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | Site: {"description":"Central gate","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"UniProtKB","id":"Q00194","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
