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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8BX7

Structure of the rod CNG channel bound to calmodulin

Functional Information from GO Data
ChainGOidnamespacecontents
A0001750cellular_componentphotoreceptor outer segment
A0005216molecular_functionmonoatomic ion channel activity
A0005221molecular_functionintracellularly cyclic nucleotide-activated monoatomic cation channel activity
A0005222molecular_functionintracellularly cAMP-activated cation channel activity
A0005223molecular_functionintracellularly cGMP-activated cation channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006812biological_processmonoatomic cation transport
A0006814biological_processsodium ion transport
A0006816biological_processcalcium ion transport
A0007606biological_processsensory perception of chemical stimulus
A0016020cellular_componentmembrane
A0017071cellular_componentintracellular cyclic nucleotide activated cation channel complex
A0030552molecular_functioncAMP binding
A0030553molecular_functioncGMP binding
A0055085biological_processtransmembrane transport
A0098655biological_processmonoatomic cation transmembrane transport
A0120200cellular_componentrod photoreceptor outer segment
A1902495cellular_componenttransmembrane transporter complex
B0001750cellular_componentphotoreceptor outer segment
B0005216molecular_functionmonoatomic ion channel activity
B0005221molecular_functionintracellularly cyclic nucleotide-activated monoatomic cation channel activity
B0005222molecular_functionintracellularly cAMP-activated cation channel activity
B0005223molecular_functionintracellularly cGMP-activated cation channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006812biological_processmonoatomic cation transport
B0006814biological_processsodium ion transport
B0006816biological_processcalcium ion transport
B0007606biological_processsensory perception of chemical stimulus
B0016020cellular_componentmembrane
B0017071cellular_componentintracellular cyclic nucleotide activated cation channel complex
B0030552molecular_functioncAMP binding
B0030553molecular_functioncGMP binding
B0055085biological_processtransmembrane transport
B0098655biological_processmonoatomic cation transmembrane transport
B0120200cellular_componentrod photoreceptor outer segment
B1902495cellular_componenttransmembrane transporter complex
C0001750cellular_componentphotoreceptor outer segment
C0005216molecular_functionmonoatomic ion channel activity
C0005221molecular_functionintracellularly cyclic nucleotide-activated monoatomic cation channel activity
C0005222molecular_functionintracellularly cAMP-activated cation channel activity
C0005223molecular_functionintracellularly cGMP-activated cation channel activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006812biological_processmonoatomic cation transport
C0006814biological_processsodium ion transport
C0006816biological_processcalcium ion transport
C0007606biological_processsensory perception of chemical stimulus
C0016020cellular_componentmembrane
C0017071cellular_componentintracellular cyclic nucleotide activated cation channel complex
C0030552molecular_functioncAMP binding
C0030553molecular_functioncGMP binding
C0055085biological_processtransmembrane transport
C0098655biological_processmonoatomic cation transmembrane transport
C0120200cellular_componentrod photoreceptor outer segment
C1902495cellular_componenttransmembrane transporter complex
D0001750cellular_componentphotoreceptor outer segment
D0001895biological_processretina homeostasis
D0005216molecular_functionmonoatomic ion channel activity
D0005221molecular_functionintracellularly cyclic nucleotide-activated monoatomic cation channel activity
D0005222molecular_functionintracellularly cAMP-activated cation channel activity
D0005223molecular_functionintracellularly cGMP-activated cation channel activity
D0005515molecular_functionprotein binding
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0006813biological_processpotassium ion transport
D0006814biological_processsodium ion transport
D0006816biological_processcalcium ion transport
D0007601biological_processvisual perception
D0007608biological_processsensory perception of smell
D0016020cellular_componentmembrane
D0017071cellular_componentintracellular cyclic nucleotide activated cation channel complex
D0030552molecular_functioncAMP binding
D0030553molecular_functioncGMP binding
D0042622cellular_componentphotoreceptor outer segment membrane
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0043855molecular_functioncyclic nucleotide-activated monoatomic ion channel activity
D0055085biological_processtransmembrane transport
D0098655biological_processmonoatomic cation transmembrane transport
D0098804cellular_componentnon-motile cilium membrane
D0099094molecular_functionligand-gated monoatomic cation channel activity
D0120200cellular_componentrod photoreceptor outer segment
E0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
EASP21-LEU33
EASP57-PHE69
EASP94-LEU106
EASP130-PHE142
site_idPS00888
Number of Residues17
DetailsCNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. ICkKGDiGReMYIIkeG
ChainResidueDetails
AILE504-GLY520
DVAL1103-GLY1119
site_idPS00889
Number of Residues24
DetailsCNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEiSIlnikgskagnrRTAnIkS
ChainResidueDetails
APHE542-SER565
DPHE1142-ALA1162
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues93
DetailsTransmembrane: {"description":"Helical; Name=S1","evidences":[{"source":"PubMed","id":"37011209","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues153
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues83
DetailsTransmembrane: {"description":"Helical; Name=S2","evidences":[{"source":"PubMed","id":"37011209","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues119
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues50
DetailsTransmembrane: {"description":"Helical; Name=S3","evidences":[{"source":"PubMed","id":"37011209","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues68
DetailsTransmembrane: {"description":"Helical; Name=S4","evidences":[{"source":"PubMed","id":"37011209","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues90
DetailsTransmembrane: {"description":"Helical; Name=S5","evidences":[{"source":"PubMed","id":"37011209","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues132
DetailsTransmembrane: {"description":"Helical; Name=P-helix","evidences":[{"source":"PubMed","id":"37011209","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues102
DetailsTransmembrane: {"description":"Helical; Name=S6","evidences":[{"source":"PubMed","id":"37011209","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8BX7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues99
DetailsRegion: {"description":"Ion conduction pathway","evidences":[{"source":"UniProtKB","id":"Q14028","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"34969975","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsRegion: {"description":"Selectivity filter","evidences":[{"source":"PubMed","id":"34969975","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues116
DetailsRegion: {"description":"Cyclic nucleotide-binding domain","evidences":[{"source":"PubMed","id":"34969975","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q14028","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsSite: {"description":"Central gate","evidences":[{"source":"PubMed","id":"34969975","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsSite: {"description":"Occludes the pore below the central gate","evidences":[{"source":"PubMed","id":"34969975","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues327
DetailsRegion: {"description":"Ion conduction pathway","evidences":[{"source":"PubMed","id":"37011209","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues9
DetailsRegion: {"description":"Selectivity filter","evidences":[{"source":"PubMed","id":"25963832","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"34969975","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues228
DetailsRegion: {"description":"C-linker","evidences":[{"source":"PubMed","id":"25963832","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues363
DetailsRegion: {"description":"Cyclic nucleotide-binding domain (CNBD)","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"25963832","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"34969975","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"37011209","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues86
DetailsCoiled coil: {"evidences":[{"source":"PubMed","id":"21878911","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"1370452","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

254227

PDB entries from 2026-05-27

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