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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 Residues21
DetailsTRANSMEM: Helical; Name=S1 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9
ChainResidueDetails
BVAL657-TRP678
ATYR166-ALA187
DTYR166-ALA187

site_idSWS_FT_FI2
Number of Residues45
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
BALA679-ASN687
BLEU745-LEU760
BTYR809-SER831
ACYS188-LEU197
ALEU263-TYR267
APHE318-PRO340
DCYS188-LEU197
DLEU263-TYR267
DPHE318-PRO340

site_idSWS_FT_FI3
Number of Residues21
DetailsTRANSMEM: Helical; Name=S2 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9
ChainResidueDetails
BILE688-PHE709
AGLU198-ARG218
DGLU198-ARG218

site_idSWS_FT_FI4
Number of Residues391
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
BGLN710-ASP724
BGLU774-LYS785
BALA885-GLU1251
ATHR219-ASN243
AARG287-ASN293
ASER401-PRO686
DTHR219-ASN243
DARG287-ASN293
DSER401-PRO686

site_idSWS_FT_FI5
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9
ChainResidueDetails
BLYS725-SER744
ALEU244-LYS262
DLEU244-LYS262

site_idSWS_FT_FI6
Number of Residues12
DetailsTRANSMEM: Helical; Name=S4 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9
ChainResidueDetails
BLEU761-PHE773
APRO268-GLN286
DPRO268-GLN286

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=S5 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9
ChainResidueDetails
BALA786-LEU808
ATYR294-VAL317
DTYR294-VAL317

site_idSWS_FT_FI8
Number of Residues26
DetailsTRANSMEM: Helical; Name=P-helix => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9
ChainResidueDetails
BTYR832-ILE858
AGLU341-TYR375
DGLU341-TYR375

site_idSWS_FT_FI9
Number of Residues25
DetailsTRANSMEM: Helical; Name=S6 => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RH9
ChainResidueDetails
BVAL859-GLY884
AVAL376-ILE400
DVAL376-ILE400

site_idSWS_FT_FI10
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RHI
ChainResidueDetails
BGLY1029
DPHE544
DALA557
DGLY558
BGLU1030
BSER1032
CGLY558
AGLY541
APHE544
AALA557
AGLY558
DGLY541

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RHH
ChainResidueDetails
BARG1042
CPHE389
AGLY385
APHE389
DGLY385
DPHE389

site_idSWS_FT_FI12
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:34699778, ECO:0007744|PDB:7RHH, ECO:0007744|PDB:7RHI
ChainResidueDetails
BTHR1043
AILE325
DILE325

site_idSWS_FT_FI13
Number of Residues2
DetailsSITE: Central gate => ECO:0000305|PubMed:34699778
ChainResidueDetails
BPHE872
BILE876

site_idSWS_FT_FI14
Number of Residues1
DetailsSITE: Occludes the pore below the central gate => ECO:0000305|PubMed:34699778
ChainResidueDetails
BARG880

226707

PDB entries from 2024-10-30

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