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8F6P

Rat Cardiac Sodium Channel with Ranolazine Bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0001518cellular_componentvoltage-gated sodium channel complex
A0003674molecular_functionmolecular_function
A0005216molecular_functionmonoatomic ion channel activity
A0005248molecular_functionvoltage-gated sodium channel activity
A0005261molecular_functionmonoatomic cation channel activity
A0005575cellular_componentcellular_component
A0005886cellular_componentplasma membrane
A0006091biological_processgeneration of precursor metabolites and energy
A0006811biological_processmonoatomic ion transport
A0006814biological_processsodium ion transport
A0008218biological_processbioluminescence
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues882
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-SER132
APHE1522-LEU1584
AGLY1633-GLY1644
AMET1693-THR1711
AARG180-PRO193
ASER235-ASP253
AVAL412-GLN915
AILE769-TRP782
ATRP823-GLY838
ATRP1260-ILE1526
APRO1312-VAL1325
AASP1372-SER1388

site_idSWS_FT_FI2
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU133-GLN151

site_idSWS_FT_FI3
Number of Residues309
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AHIS152-THR158
AILE1345-ILE1352
AALA1409-SER1460
AGLY1483-MET1499
ALEU1603-ILE1613
AGLY1663-ILE1675
ACYS1730-ILE1751
AGLU1775-PHE1803
AASP212-SER217
AMET274-SER358
AARG384-TYR390
AGLU738-GLU748
AGLY803-ASN804
AGLY858-ASP886
AASP908-LEU920
AILE1280-THR1292

site_idSWS_FT_FI4
Number of Residues20
DetailsTRANSMEM: Helical; Name=S2 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALYS159-ALA179

site_idSWS_FT_FI5
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATRP194-VAL211

site_idSWS_FT_FI6
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AALA218-ILE234

site_idSWS_FT_FI7
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL254-PHE273

site_idSWS_FT_FI8
Number of Residues87
DetailsINTRAMEM: Pore-forming => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE359-LEU383
APHE887-TRP907
APHE1461-LEU1482
ALEU1752-LEU1774

site_idSWS_FT_FI9
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET391-ALA411

site_idSWS_FT_FI10
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE719-LEU737

site_idSWS_FT_FI11
Number of Residues19
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET749-LYS768

site_idSWS_FT_FI12
Number of Residues19
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AASN783-MET802

site_idSWS_FT_FI13
Number of Residues17
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU805-SER822

site_idSWS_FT_FI14
Number of Residues18
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AALA839-VAL857

site_idSWS_FT_FI15
Number of Residues20
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL921-LEU941

site_idSWS_FT_FI16
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AALA1262-LEU1279

site_idSWS_FT_FI17
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1293-ARG1311

site_idSWS_FT_FI18
Number of Residues18
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL1326-LEU1344

site_idSWS_FT_FI19
Number of Residues18
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET1353-GLY1371

site_idSWS_FT_FI20
Number of Residues19
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1389-GLY1408

site_idSWS_FT_FI21
Number of Residues21
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET1500-GLY1521

site_idSWS_FT_FI22
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AARG1585-ILE1602

site_idSWS_FT_FI23
Number of Residues18
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1614-ILE1632

site_idSWS_FT_FI24
Number of Residues17
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1645-ILE1662

site_idSWS_FT_FI25
Number of Residues16
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
APHE1676-ASP1692

site_idSWS_FT_FI26
Number of Residues17
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ASER1712-TYR1729

site_idSWS_FT_FI27
Number of Residues22
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AASP1804-PRO1826

site_idSWS_FT_FI28
Number of Residues1
DetailsSITE: Cys residue near the selectivity filter, which has a free thiol that is susceptible to reaction with methanethiosulfonate (MTSET); Sodium current is irreversibly blocked by MTSET => ECO:0000250|UniProtKB:P04775, ECO:0000269|PubMed:26039939
ChainResidueDetails
ACYS374

site_idSWS_FT_FI29
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q14524
ChainResidueDetails
ASER37
ASER655
ASER658
ATYR695
ALYS708
AILE769
ASER665
ASER668

site_idSWS_FT_FI30
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q14524
ChainResidueDetails
ATHR39

site_idSWS_FT_FI31
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
AHIS681
AARG682

site_idSWS_FT_FI32
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:22673903
ChainResidueDetails
ACYS684

site_idSWS_FT_FI33
Number of Residues1
DetailsMOD_RES: Omega-N-methylarginine; alternate => ECO:0000250|UniProtKB:Q14524
ChainResidueDetails
AILE724

site_idSWS_FT_FI34
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9JJV9
ChainResidueDetails
ALEU737

site_idSWS_FT_FI35
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKC => ECO:0000250|UniProtKB:Q14524
ChainResidueDetails
ALYS1558

site_idSWS_FT_FI36
Number of Residues13
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN215
APHE1420
AALA1429
AGLY1435
AGLU1443
AASN284
AASN289
AASN292
AASN319
AASN329
AASN741
AASN804
AASN865

site_idSWS_FT_FI37
Number of Residues1
DetailsMOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132
ChainResidueDetails
ATYR1974

site_idSWS_FT_FI38
Number of Residues2
DetailsCROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132
ChainResidueDetails
ATHR1973
AGLY1975

222415

PDB entries from 2024-07-10

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