Rat Cardiac Sodium Channel with Ranolazine Bound. Determined by electron microscopy at 3.2 Å resolution. Released 12 Apr 2023.
Explore 8F6P in 3D Show helices and sheets RCSB PDB PDBe
8F6P contains 65 α-helices and 12 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 120-130 | 11 | |
| α-helix | 132-149 | 18 | |
| α-helix | 156-179 | 24 | |
| α-helix | 195-210 | 16 | |
| α-helix | 218-228 | 11 | |
| α-helix | 229-233 | 5 | |
| α-helix | 235-250 | 16 | |
| α-helix | 252-272 | 21 | |
| α-helix | 276-278 | 3 | |
| β-strand | 280-283 | 4 | 1 |
| β-strand | 287 | 1 | 2 |
| β-strand | 295 | 1 | 2 |
| α-helix | 297-299 | 3 | |
| β-strand | 302 | 1 | 2 |
| α-helix | 305-310 | 6 | |
| α-helix | 312-314 | 3 | |
| β-strand | 317 | 1 | 3 |
| α-helix | 318 | 1 | |
| β-strand | 324 | 1 | 3 |
| α-helix | 336-337 | 2 | |
| β-strand | 340-343 | 4 | 1 |
| α-helix | 350-352 | 3 | |
| α-helix | 359-370 | 12 | |
| α-helix | 375-385 | 11 | |
| α-helix | 388-390 | 3 | |
| α-helix | 391-397 | 7 | |
| α-helix | 398-402 | 5 | |
| α-helix | 403-429 | 27 | |
| α-helix | 720-736 | 17 | |
| α-helix | 744-771 | 28 | |
| α-helix | 774-777 | 4 | |
| α-helix | 781-797 | 17 | |
| α-helix | 807-809 | 3 | |
| α-helix | 810-813 | 4 | |
| α-helix | 814-821 | 8 | |
| α-helix | 824-836 | 13 | |
| α-helix | 841-868 | 28 | |
| α-helix | 870-873 | 4 | |
| α-helix | 887-899 | 13 | |
| α-helix | 904-912 | 9 | |
| α-helix | 915-944 | 30 | |
| α-helix | 1194-1205 | 12 | |
| α-helix | 1207-1224 | 18 | |
| α-helix | 1236-1269 | 34 | |
| α-helix | 1272-1291 | 20 | |
| α-helix | 1302-1305 | 4 | |
| α-helix | 1306-1315 | 10 | |
| α-helix | 1320-1358 | 39 | |
| β-strand | 1363-1367 | 5 | 4 |
| β-strand | 1374 | 1 | 4 |
| α-helix | 1375-1376 | 2 | |
| β-strand | 1382 | 1 | 5 |
| α-helix | 1383-1388 | 6 | |
| β-strand | 1395-1399 | 5 | 4 |
| α-helix | 1408-1418 | 11 | |
| α-helix | 1423-1430 | 8 | |
| β-strand | 1438 | 1 | 5 |
| α-helix | 1439-1441 | 3 | |
| α-helix | 1448-1455 | 8 | |
| α-helix | 1456-1462 | 7 | |
| α-helix | 1463-1481 | 19 | |
| α-helix | 1491-1504 | 14 | |
| α-helix | 1506-1508 | 3 | |
| α-helix | 1521-1527 | 7 | |
| α-helix | 1530-1548 | 19 | |
| α-helix | 1556-1581 | 26 | |
| α-helix | 1586-1590 | 5 | |
| α-helix | 1592-1611 | 20 | |
| α-helix | 1623-1629 | 7 | |
| α-helix | 1630-1637 | 8 | |
| α-helix | 1638-1641 | 4 | |
| α-helix | 1644-1680 | 37 | |
| α-helix | 1699-1710 | 12 | |
| α-helix | 1715-1723 | 9 | |
| α-helix | 1747-1761 | 15 | |
| α-helix | 1762-1768 | 7 | |
| α-helix | 1769-1779 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 5 subunit alpha,Green fluorescent protein | A | protein | 1838 | Rattus norvegicus, Aequorea victoria | P15389 (AlphaFold model), P42212 (AlphaFold model) |
>8F6P_1 Sodium channel protein type 5 subunit alpha,Green fluorescent protein (chains A) MANLLLPRGTSSFRRFTRESLAAIEKRMAEKQARGGSATSQESREGLQEEEAPRPQLDLQ ASKKLPDLYGNPPRELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHP VRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILAR GFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTI VGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGL VWNSLDVYLNDPANYLLKNGTTDVLLCGNSSDAGTCPEGYRCLKAGQNPDHGYTSFDSFA WAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQ NQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSARQRALSAVSVLTSALEEL EESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFADLTITMCIVLNTLFMAL EHYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMEL GLSRMGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVV GMQLFGKNYSELRHRISDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSL CLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMNNLQLALARIQRGLRFVK RTTWDFCCGILRRRPKKPAALATHSQLPSCITAPRSPPPPEVEKVPPARKETRFEEDKRP GQGTPGDSEPVCVPIAVAESDTEDQEEDEENGKVWWRLRKTCYRIVEHSWFETFIIFMIL LSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDF LIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMN VLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWT KVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEDNLYMYIYFVVFIIF GSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNMMKKLGSKKPQKPIPRPLNK YQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECI VKMAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRL IRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQT FANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYI IISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSD FADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQME EKFMAANPSKISYEPITTTLEVLFQGPGSMVSKGEELFTGVVPILVELDGDVNGHKFSVS GEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPE GYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNV YIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKD PNEKRDHMVLLEFVTAAGITLGMDELYKGSDYKDDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 13 |
| 6OU | [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-y… | C39 H76 N O8 P | 6 |
| XHO | (R)-ranolazine | C24 H33 N3 O4 | 1 |
| BMA | beta-D-mannopyranose | C6 H12 O6 | 3 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 7 |
Structural basis for inhibition of the cardiac sodium channel by the atypical antiarrhythmic drug ranolazine. Lenaeus, M., Gamal El-Din, T.M., Tonggu, L. et al. Nat Cardiovasc Res (2023) 2:587-594. DOI 10.1038/s44161-023-00271-5 · PubMed
Other PDB entries of the same protein (UniProt P15389 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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