Structure of full-length human cardiac sodium channel - Class-II. Determined by electron microscopy at 3.9 Å resolution. Released 12 Feb 2025.
Explore 8VYK in 3D Show helices and sheets RCSB PDB PDBe
8VYK contains 80 α-helices and 18 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 | 18-25 | 8 | |
| α-helix | 28-30 | 3 | |
| α-helix | 31-35 | 5 | |
| β-strand | 80 | 1 | 1 |
| β-strand | 92-96 | 5 | 1 |
| β-strand | 102-106 | 5 | 1 |
| α-helix | 119-129 | 11 | |
| α-helix | 131-147 | 17 | |
| α-helix | 157-179 | 23 | |
| α-helix | 198-209 | 12 | |
| α-helix | 211-212 | 2 | |
| α-helix | 221-231 | 11 | |
| α-helix | 234-249 | 16 | |
| α-helix | 254-269 | 16 | |
| β-strand | 278-282 | 5 | 2 |
| α-helix | 283-284 | 2 | |
| β-strand | 294-296 | 3 | 3 |
| β-strand | 299-301 | 3 | 3 |
| α-helix | 305-308 | 4 | |
| α-helix | 311-313 | 3 | |
| β-strand | 314 | 1 | 2 |
| α-helix | 315 | 1 | |
| β-strand | 316 | 1 | 4 |
| β-strand | 323 | 1 | 4 |
| α-helix | 324-325 | 2 | |
| α-helix | 335-336 | 2 | |
| β-strand | 339-343 | 5 | 2 |
| α-helix | 346-347 | 2 | |
| α-helix | 349-351 | 3 | |
| α-helix | 358-370 | 13 | |
| α-helix | 374-385 | 12 | |
| α-helix | 387-389 | 3 | |
| α-helix | 390-397 | 8 | |
| α-helix | 398-402 | 5 | |
| α-helix | 403-432 | 30 | |
| α-helix | 689-692 | 4 | |
| α-helix | 706-713 | 8 | |
| α-helix | 719-733 | 15 | |
| α-helix | 745-766 | 22 | |
| α-helix | 773-775 | 3 | |
| α-helix | 781-795 | 15 | |
| α-helix | 805-817 | 13 | |
| α-helix | 825-833 | 9 | |
| α-helix | 834-838 | 5 | |
| α-helix | 840-861 | 22 | |
| α-helix | 866-868 | 3 | |
| α-helix | 884-895 | 12 | |
| α-helix | 900-903 | 4 | |
| α-helix | 915-942 | 28 | |
| α-helix | 1163-1165 | 3 | |
| α-helix | 1172-1175 | 4 | |
| α-helix | 1186-1188 | 3 | |
| α-helix | 1189-1203 | 15 | |
| α-helix | 1205-1221 | 17 | |
| α-helix | 1222-1224 | 3 | |
| α-helix | 1227-1230 | 4 | |
| α-helix | 1234-1260 | 27 | |
| α-helix | 1271-1290 | 20 | |
| α-helix | 1297-1301 | 5 | |
| α-helix | 1302-1316 | 15 | |
| α-helix | 1318-1327 | 10 | |
| α-helix | 1331-1356 | 26 | |
| β-strand | 1361-1365 | 5 | 5 |
| β-strand | 1380 | 1 | 6 |
| α-helix | 1381-1386 | 6 | |
| β-strand | 1393-1397 | 5 | 5 |
| α-helix | 1405-1417 | 13 | |
| α-helix | 1421-1429 | 9 | |
| β-strand | 1436 | 1 | 6 |
| α-helix | 1444-1446 | 3 | |
| α-helix | 1447-1454 | 8 | |
| α-helix | 1455-1459 | 5 | |
| α-helix | 1460-1480 | 21 | |
| α-helix | 1489-1497 | 9 | |
| α-helix | 1518-1526 | 9 | |
| α-helix | 1529-1544 | 16 | |
| α-helix | 1554-1577 | 24 | |
| α-helix | 1593-1606 | 14 | |
| α-helix | 1608-1611 | 4 | |
| α-helix | 1621-1626 | 6 | |
| α-helix | 1627-1630 | 4 | |
| α-helix | 1634-1637 | 4 | |
| α-helix | 1645-1653 | 9 | |
| α-helix | 1655-1675 | 21 | |
| α-helix | 1697-1707 | 11 | |
| α-helix | 1714-1717 | 4 | |
| α-helix | 1718-1720 | 3 | |
| α-helix | 1745-1775 | 31 | |
| α-helix | 1791-1801 | 11 | |
| β-strand | 1808-1809 | 2 | 7 |
| α-helix | 1811-1817 | 7 | |
| α-helix | 1818-1820 | 3 | |
| α-helix | 1832-1835 | 4 | |
| β-strand | 1843 | 1 | 8 |
| β-strand | 1847 | 1 | 8 |
| β-strand | 1848-1849 | 2 | 7 |
| α-helix | 1854-1859 | 6 | |
| α-helix | 1867-1881 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 5 subunit alpha | A | protein | 2016 | Homo sapiens | Q14524 (AlphaFold model) |
>8VYK_1 Sodium channel protein type 5 subunit alpha (chains A) MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQA SKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPI RRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARG FCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIV GALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLV WESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAW AFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQN QATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRK RMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSE ADFADDENSTAGESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGV VSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQ RALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTD LTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQG WNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALG NLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWI ETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQ LALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVP PTRKETRFEEGEQPGQGTPGDPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQQESQ PVSGGPEAPPDSRTWSQVSATASSEAEASASQADWRQQWKAEPQAPGCGETPEDSCSEGS TADMTNTAELLEQIPDLGQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYH IVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVA YGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGM RVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNN KSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQW EYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKK LGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINIL AKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPT LFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFA YVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRG DCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEK FDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKR VLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRS LKHASFLFRQQAGSGLSEEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSV TRATSDNLQVRGSDYSHSEDLADFPPSPDRDRESIV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6OU | [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-y… | C39 H76 N O8 P | 2 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 7 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Structural basis of human Na v 1.5 gating mechanisms. Biswas, R., Lopez-Serrano, A.L., Purohit, A. et al. Proc Natl Acad Sci U S A (2025) 122:e2416181122-e2416181122. DOI 10.1073/pnas.2416181122 · PubMed
Other PDB entries of the same protein (UniProt Q14524 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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