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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7RHK

Cryo-EM structure of human rod CNGA1/B1 channel in L-cis-Diltiazem-trapped closed state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005221molecular_functionintracellularly cyclic nucleotide-activated monoatomic cation channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
B0005221molecular_functionintracellularly cyclic nucleotide-activated monoatomic cation channel activity
C0005216molecular_functionmonoatomic ion channel activity
C0005221molecular_functionintracellularly cyclic nucleotide-activated monoatomic cation channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0055085biological_processtransmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005221molecular_functionintracellularly cyclic nucleotide-activated monoatomic cation channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0055085biological_processtransmembrane transport
Functional Information from PROSITE/UniProt
site_idPS00888
Number of Residues17
DetailsCNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VCkKGEiGReMYIIqaG
ChainResidueDetails
BVAL989-GLY1005
CILE506-GLY522
site_idPS00889
Number of Residues21
DetailsCNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEiSLlavgggnr...RTAnVvA
ChainResidueDetails
BPHE1028-ALA1048
CPHE544-SER567
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues84
DetailsTransmembrane: {"description":"Helical; Name=S1","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues113
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues81
DetailsTransmembrane: {"description":"Helical; Name=S2","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues115
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues73
DetailsTransmembrane: {"description":"Helical; Name=S3","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues66
DetailsTransmembrane: {"description":"Helical; Name=S4","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues91
DetailsTransmembrane: {"description":"Helical; Name=S5","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues128
DetailsTransmembrane: {"description":"Helical; Name=P-helix","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues97
DetailsTransmembrane: {"description":"Helical; Name=S6","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues324
DetailsRegion: {"description":"Ion conduction pathway","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues9
DetailsRegion: {"description":"Selectivity filter","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues304
DetailsRegion: {"description":"C-linker","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues476
DetailsRegion: {"description":"Cyclic nucleotide-binding domain","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7RHI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RHH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues8
DetailsSite: {"description":"Central gate","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"UniProtKB","id":"Q00194","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RHI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RHH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7RHI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsSite: {"description":"Occludes the pore below the central gate","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

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PDB entries from 2025-07-16

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