Structure of human cardiac sodium channel Nav1.5 in intermediate open state. Determined by electron microscopy at 3.48 Å resolution. Released 8 Apr 2026.
Explore 9P24 in 3D Show helices and sheets RCSB PDB PDBe
9P24 contains 64 α-helices and 22 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 | 18-36 | 19 | |
| α-helix | 53-55 | 3 | |
| β-strand | 63 | 1 | 1 |
| α-helix | 64-65 | 2 | |
| β-strand | 80 | 1 | 2 |
| α-helix | 86-89 | 4 | |
| β-strand | 92-93 | 2 | 3 |
| β-strand | 94 | 1 | 2 |
| β-strand | 101 | 1 | 1 |
| β-strand | 105-106 | 2 | 3 |
| α-helix | 109-110 | 2 | |
| α-helix | 119-129 | 11 | |
| α-helix | 132-146 | 15 | |
| α-helix | 157-178 | 22 | |
| α-helix | 188-190 | 3 | |
| α-helix | 193-209 | 17 | |
| α-helix | 224-227 | 4 | |
| α-helix | 236-249 | 14 | |
| α-helix | 254-269 | 16 | |
| β-strand | 278-282 | 5 | 4 |
| β-strand | 285 | 1 | 5 |
| β-strand | 295-296 | 2 | 5 |
| β-strand | 299-300 | 2 | 5 |
| α-helix | 304-309 | 6 | |
| β-strand | 316 | 1 | 6 |
| α-helix | 317 | 1 | |
| β-strand | 323 | 1 | 6 |
| β-strand | 339-343 | 5 | 4 |
| α-helix | 349-351 | 3 | |
| α-helix | 358-370 | 13 | |
| α-helix | 374-384 | 11 | |
| α-helix | 390-400 | 11 | |
| α-helix | 404-438 | 35 | |
| α-helix | 703-714 | 12 | |
| α-helix | 720-734 | 15 | |
| β-strand | 738 | 1 | 7 |
| α-helix | 743-775 | 33 | |
| α-helix | 780-793 | 14 | |
| α-helix | 805-820 | 16 | |
| α-helix | 823-834 | 12 | |
| α-helix | 843-860 | 18 | |
| α-helix | 863-871 | 9 | |
| α-helix | 884-896 | 13 | |
| α-helix | 901-910 | 10 | |
| α-helix | 913-942 | 30 | |
| α-helix | 959-970 | 12 | |
| α-helix | 1189-1202 | 14 | |
| α-helix | 1205-1220 | 16 | |
| α-helix | 1221-1224 | 4 | |
| α-helix | 1236-1261 | 26 | |
| α-helix | 1263-1266 | 4 | |
| α-helix | 1270-1290 | 21 | |
| α-helix | 1297-1303 | 7 | |
| α-helix | 1304-1314 | 11 | |
| α-helix | 1318-1328 | 11 | |
| α-helix | 1332-1355 | 24 | |
| β-strand | 1361-1364 | 4 | 8 |
| α-helix | 1371 | 1 | |
| β-strand | 1372 | 1 | 8 |
| α-helix | 1373-1374 | 2 | |
| β-strand | 1380 | 1 | 9 |
| α-helix | 1381-1386 | 6 | |
| β-strand | 1394-1397 | 4 | 8 |
| β-strand | 1404 | 1 | 7 |
| α-helix | 1405-1416 | 12 | |
| α-helix | 1421-1429 | 9 | |
| β-strand | 1436 | 1 | 9 |
| α-helix | 1444-1446 | 3 | |
| α-helix | 1447-1456 | 10 | |
| α-helix | 1460-1479 | 20 | |
| α-helix | 1489-1502 | 14 | |
| α-helix | 1505-1508 | 4 | |
| α-helix | 1519-1525 | 7 | |
| α-helix | 1528-1545 | 18 | |
| α-helix | 1554-1581 | 28 | |
| α-helix | 1592-1615 | 24 | |
| α-helix | 1619-1626 | 8 | |
| α-helix | 1627-1630 | 4 | |
| α-helix | 1634-1639 | 6 | |
| α-helix | 1642-1653 | 12 | |
| α-helix | 1655-1676 | 22 | |
| α-helix | 1697-1707 | 11 | |
| α-helix | 1713-1717 | 5 | |
| β-strand | 1733 | 1 | 10 |
| β-strand | 1739 | 1 | 10 |
| α-helix | 1745-1777 | 33 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 5 subunit alpha | A | protein | 2016 | Homo sapiens | Q14524 (AlphaFold model) |
>9P24_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 |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 8 |
| 9Z9 | (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en | C34 H56 O5 | 1 |
Water and common crystallization additives (NA) are not listed.
Structural and functional mechanisms underlying activation gate dynamics and IFM motif accessibility in human Na v 1.5. Biswas, R., Lopez-Serrano, A.L., Purohit, A. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-69672-x · 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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