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8F6P

Rat Cardiac Sodium Channel with Ranolazine Bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0001518cellular_componentvoltage-gated sodium channel complex
A0005216molecular_functionmonoatomic ion channel activity
A0005248molecular_functionvoltage-gated sodium channel activity
A0005261molecular_functionmonoatomic cation channel activity
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 Residues829
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-VAL130
AILE1526-ALA1583
ALEU1636-GLY1644
APHE1696-CYS1705
AGLY181-PHE189
ALYS238-LYS250
AMET415-LEU917
AALA771-TYR776
ATRP823-ALA839
ATYR1263-ILE1523
AALA1315-ARG1323
ALEU1373-GLU1385

site_idSWS_FT_FI2
Number of Residues19
DetailsTRANSMEM: Helical; Name=S1 of repeat I => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
AHIS131-ALA150

site_idSWS_FT_FI3
Number of Residues298
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AGLN151-THR158
ATRP1347-ILE1352
ATYR1411-PHE1455
AGLN1478-MET1500
ALEU1603-ILE1613
ALEU1668-SER1674
APRO1735-LEU1752
AILE1770-TRP1800
AVAL211-SER217
AMET274-SER358
AGLN380-GLY387
AHIS739-GLU747
AGLY798-VAL807
APHE862-PHE887
ATRP907-GLN915
AVAL1281-ASN1291

site_idSWS_FT_FI4
Number of Residues21
DetailsTRANSMEM: Helical; Name=S2 of repeat I => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
ALYS159-ARG180

site_idSWS_FT_FI5
Number of Residues20
DetailsTRANSMEM: Helical; Name=S3 of repeat I => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
ALEU190-PHE210

site_idSWS_FT_FI6
Number of Residues19
DetailsTRANSMEM: Helical; Name=S4 of repeat I => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
AALA218-LEU237

site_idSWS_FT_FI7
Number of Residues22
DetailsTRANSMEM: Helical; Name=S5 of repeat I => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
ALEU251-PHE273

site_idSWS_FT_FI8
Number of Residues75
DetailsINTRAMEM: Pore-forming => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
APHE359-TYR379
APHE888-MET906
AILE1456-GLN1477
APHE1753-TYR1769

site_idSWS_FT_FI9
Number of Residues26
DetailsTRANSMEM: Helical; Name=S6 of repeat I => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
ALYS388-ALA414

site_idSWS_FT_FI10
Number of Residues17
DetailsTRANSMEM: Helical; Name=S1 of repeat II => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
AASP721-GLU738

site_idSWS_FT_FI11
Number of Residues22
DetailsTRANSMEM: Helical; Name=S2 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AGLU748-ILE770

site_idSWS_FT_FI12
Number of Residues20
DetailsTRANSMEM: Helical; Name=S3 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATYR777-LEU797

site_idSWS_FT_FI13
Number of Residues14
DetailsTRANSMEM: Helical; Name=S4 of repeat II => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
ALEU808-SER822

site_idSWS_FT_FI14
Number of Residues21
DetailsTRANSMEM: Helical; Name=S5 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU840-LEU861

site_idSWS_FT_FI15
Number of Residues28
DetailsTRANSMEM: Helical; Name=S6 of repeat II => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ASER916-SER944

site_idSWS_FT_FI16
Number of Residues21
DetailsTRANSMEM: Helical; Name=S1 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALYS1259-ILE1280

site_idSWS_FT_FI17
Number of Residues22
DetailsTRANSMEM: Helical; Name=S2 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ATHR1292-ARG1314

site_idSWS_FT_FI18
Number of Residues22
DetailsTRANSMEM: Helical; Name=S3 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AVAL1324-PHE1346

site_idSWS_FT_FI19
Number of Residues19
DetailsTRANSMEM: Helical; Name=S4 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AMET1353-ASP1372

site_idSWS_FT_FI20
Number of Residues24
DetailsTRANSMEM: Helical; Name=S5 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ACYS1386-GLY1410

site_idSWS_FT_FI21
Number of Residues24
DetailsTRANSMEM: Helical; Name=S6 of repeat III => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALYS1501-ASP1525

site_idSWS_FT_FI22
Number of Residues18
DetailsTRANSMEM: Helical; Name=S1 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
ALEU1584-ILE1602

site_idSWS_FT_FI23
Number of Residues21
DetailsTRANSMEM: Helical; Name=S2 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1614-ILE1635

site_idSWS_FT_FI24
Number of Residues22
DetailsTRANSMEM: Helical; Name=S3 of repeat IV => ECO:0000250|UniProtKB:D0E0C2
ChainResidueDetails
AILE1645-PHE1667

site_idSWS_FT_FI25
Number of Residues20
DetailsTRANSMEM: Helical; Name=S4 of repeat IV => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
AILE1675-ASN1695

site_idSWS_FT_FI26
Number of Residues28
DetailsTRANSMEM: Helical; Name=S5 of repeat IV => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
ALEU1706-LEU1734

site_idSWS_FT_FI27
Number of Residues25
DetailsTRANSMEM: Helical; Name=S6 of repeat IV => ECO:0000305|PubMed:31866066, ECO:0007744|PDB:6UZ0
ChainResidueDetails
AGLU1801-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 Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN215
AALA1429
AGLY1435
AGLU1443
AASN284
AASN289
AASN292
AASN329
AASN741
AASN804
AASN865
APHE1420

site_idSWS_FT_FI37
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31866066, ECO:0007744|PDB:6UZ0, ECO:0007744|PDB:6UZ3
ChainResidueDetails
AASN319

site_idSWS_FT_FI38
Number of Residues1
DetailsMOD_RES: (Z)-2,3-didehydrotyrosine => ECO:0000269|PubMed:8448132
ChainResidueDetails
ATYR1974

site_idSWS_FT_FI39
Number of Residues2
DetailsCROSSLNK: 5-imidazolinone (Ser-Gly) => ECO:0000269|PubMed:8448132
ChainResidueDetails
ATHR1973
AGLY1975

237992

PDB entries from 2025-06-25

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