Structure of full-length human cardiac sodium channel - Class-I. Determined by electron microscopy at 3.6 Å resolution. Released 12 Feb 2025.
Explore 8VYJ in 3D Show helices and sheets RCSB PDB PDBe
8VYJ contains 75 α-helices and 17 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 | 22-28 | 7 | |
| α-helix | 31-35 | 5 | |
| β-strand | 79 | 1 | 1 |
| α-helix | 86-88 | 3 | |
| β-strand | 92-95 | 4 | 1 |
| β-strand | 103-106 | 4 | 1 |
| α-helix | 119-129 | 11 | |
| α-helix | 132-147 | 16 | |
| α-helix | 157-179 | 23 | |
| α-helix | 195-206 | 12 | |
| α-helix | 207-209 | 3 | |
| α-helix | 211-213 | 3 | |
| α-helix | 219-221 | 3 | |
| α-helix | 225-231 | 7 | |
| α-helix | 234-244 | 11 | |
| α-helix | 253-269 | 17 | |
| β-strand | 278-282 | 5 | 2 |
| β-strand | 294-296 | 3 | 3 |
| β-strand | 299-301 | 3 | 3 |
| α-helix | 311-313 | 3 | |
| β-strand | 339-343 | 5 | 2 |
| α-helix | 346-347 | 2 | |
| α-helix | 349-351 | 3 | |
| α-helix | 358-370 | 13 | |
| α-helix | 375-385 | 11 | |
| α-helix | 387-389 | 3 | |
| α-helix | 390-397 | 8 | |
| α-helix | 398-402 | 5 | |
| α-helix | 403-432 | 30 | |
| α-helix | 689-694 | 6 | |
| α-helix | 706-713 | 8 | |
| α-helix | 716-720 | 5 | |
| α-helix | 721-735 | 15 | |
| α-helix | 743-770 | 28 | |
| α-helix | 773-776 | 4 | |
| α-helix | 781-797 | 17 | |
| α-helix | 811-819 | 9 | |
| α-helix | 825-834 | 10 | |
| α-helix | 840-861 | 22 | |
| α-helix | 862-864 | 3 | |
| α-helix | 876-877 | 2 | |
| α-helix | 884-896 | 13 | |
| α-helix | 900-905 | 6 | |
| α-helix | 915-942 | 28 | |
| α-helix | 1163-1165 | 3 | |
| α-helix | 1172-1174 | 3 | |
| α-helix | 1186-1203 | 18 | |
| α-helix | 1205-1220 | 16 | |
| α-helix | 1221-1224 | 4 | |
| α-helix | 1227-1229 | 3 | |
| α-helix | 1236-1260 | 25 | |
| α-helix | 1270-1290 | 21 | |
| α-helix | 1299-1304 | 6 | |
| α-helix | 1305-1314 | 10 | |
| α-helix | 1320-1328 | 9 | |
| α-helix | 1331-1355 | 25 | |
| β-strand | 1362-1365 | 4 | 4 |
| β-strand | 1372 | 1 | 4 |
| β-strand | 1380 | 1 | 5 |
| α-helix | 1381-1386 | 6 | |
| β-strand | 1393-1396 | 4 | 4 |
| α-helix | 1405-1416 | 12 | |
| α-helix | 1421-1429 | 9 | |
| β-strand | 1436 | 1 | 5 |
| α-helix | 1444-1446 | 3 | |
| α-helix | 1447-1457 | 11 | |
| α-helix | 1460-1480 | 21 | |
| α-helix | 1489-1499 | 11 | |
| α-helix | 1515-1519 | 5 | |
| α-helix | 1522-1526 | 5 | |
| α-helix | 1528-1546 | 19 | |
| α-helix | 1554-1576 | 23 | |
| α-helix | 1593-1595 | 3 | |
| α-helix | 1596-1600 | 5 | |
| α-helix | 1601-1610 | 10 | |
| α-helix | 1620-1626 | 7 | |
| α-helix | 1627-1639 | 13 | |
| α-helix | 1643-1675 | 33 | |
| β-strand | 1689 | 1 | 6 |
| β-strand | 1692 | 1 | 6 |
| α-helix | 1697-1707 | 11 | |
| α-helix | 1714-1717 | 4 | |
| α-helix | 1745-1776 | 32 | |
| α-helix | 1792-1801 | 10 | |
| β-strand | 1808-1809 | 2 | 7 |
| α-helix | 1811-1817 | 7 | |
| α-helix | 1829-1833 | 5 | |
| α-helix | 1834-1837 | 4 | |
| β-strand | 1842-1843 | 2 | 7 |
| β-strand | 1847-1849 | 3 | 7 |
| α-helix | 1850-1859 | 10 | |
| α-helix | 1869-1881 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 5 subunit alpha | A | protein | 2016 | Homo sapiens | Q14524 (AlphaFold model) |
>8VYJ_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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