Nav1.5 in complex with quinidine-azo. Determined by electron microscopy at 3.0 Å resolution. Released 1 Apr 2026.
Explore 9V3S in 3D Show helices and sheets RCSB PDB PDBe
9V3S contains 63 α-helices and 14 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 | 121-128 | 8 | |
| α-helix | 131-148 | 18 | |
| α-helix | 157-180 | 24 | |
| α-helix | 192-206 | 15 | |
| α-helix | 222-231 | 10 | |
| α-helix | 235-248 | 14 | |
| α-helix | 251-272 | 22 | |
| β-strand | 278-282 | 5 | 1 |
| β-strand | 296 | 1 | 2 |
| β-strand | 300 | 1 | 2 |
| α-helix | 304-309 | 6 | |
| β-strand | 316 | 1 | 3 |
| α-helix | 317 | 1 | |
| β-strand | 323 | 1 | 3 |
| β-strand | 339-343 | 5 | 1 |
| α-helix | 349-351 | 3 | |
| α-helix | 358-370 | 13 | |
| α-helix | 374-385 | 12 | |
| α-helix | 387-389 | 3 | |
| α-helix | 390-396 | 7 | |
| α-helix | 397-402 | 6 | |
| α-helix | 403-428 | 26 | |
| α-helix | 700-714 | 15 | |
| α-helix | 717-735 | 19 | |
| β-strand | 738 | 1 | 4 |
| α-helix | 741-742 | 2 | |
| α-helix | 745-770 | 26 | |
| α-helix | 773-776 | 4 | |
| α-helix | 782-797 | 16 | |
| α-helix | 809-820 | 12 | |
| α-helix | 825-836 | 12 | |
| α-helix | 842-861 | 20 | |
| α-helix | 867-870 | 4 | |
| α-helix | 885-896 | 12 | |
| α-helix | 900-910 | 11 | |
| α-helix | 912-938 | 27 | |
| α-helix | 939-943 | 5 | |
| α-helix | 1189-1202 | 14 | |
| α-helix | 1205-1221 | 17 | |
| α-helix | 1222-1224 | 3 | |
| α-helix | 1229-1232 | 4 | |
| α-helix | 1236-1266 | 31 | |
| α-helix | 1272-1286 | 15 | |
| α-helix | 1287-1291 | 5 | |
| α-helix | 1299-1304 | 6 | |
| α-helix | 1305-1312 | 8 | |
| α-helix | 1313-1316 | 4 | |
| α-helix | 1318-1356 | 39 | |
| β-strand | 1361-1364 | 4 | 5 |
| β-strand | 1380 | 1 | 6 |
| α-helix | 1381-1384 | 4 | |
| β-strand | 1394-1397 | 4 | 5 |
| β-strand | 1404 | 1 | 4 |
| α-helix | 1405-1416 | 12 | |
| α-helix | 1421-1424 | 4 | |
| β-strand | 1436 | 1 | 6 |
| α-helix | 1445-1453 | 9 | |
| α-helix | 1454-1460 | 7 | |
| α-helix | 1461-1479 | 19 | |
| α-helix | 1489-1501 | 13 | |
| α-helix | 1506-1508 | 3 | |
| α-helix | 1516-1526 | 11 | |
| α-helix | 1528-1545 | 18 | |
| α-helix | 1554-1581 | 28 | |
| α-helix | 1585-1588 | 4 | |
| α-helix | 1592-1612 | 21 | |
| α-helix | 1618-1628 | 11 | |
| α-helix | 1630-1633 | 4 | |
| α-helix | 1634-1637 | 4 | |
| α-helix | 1641-1678 | 38 | |
| β-strand | 1682 | 1 | 7 |
| α-helix | 1697-1708 | 12 | |
| α-helix | 1713-1720 | 8 | |
| β-strand | 1741 | 1 | 7 |
| α-helix | 1745-1759 | 15 | |
| α-helix | 1760-1766 | 7 | |
| α-helix | 1767-1780 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 5 subunit alpha | A | protein | 1618 | Homo sapiens | Q14524 (AlphaFold model) |
>9V3S_1 Sodium channel protein type 5 subunit alpha (chains A) MASWSHPQFEKGGGARGGSGGGSWSHPQFEKGFDYKDDDDKGTMANFLLPRGTSSFRRFT RESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIG EPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLI MCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLD FSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLT VFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLK NGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERL YQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEA MEMLKKEHEALTIRGVDTVSRSSARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRY LIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNL VFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLR VFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSG LLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLF LALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAA LAAQGQLPSCIATPYSPPPPETEKVPPTRKETRFEEGEQPGQGTPGDPEPVCVPIAVAES DTDDQEEDEENGKVWWRLRKTCYHIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIK VLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEM GPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLF AGKFGRCINQTEGDLPLNYTIVNNKSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVA TFKGWMDIMYAAVDSRGYEEQPQWEYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQ KKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMF LICLNMVTMMVETDDQSPEKINILAKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDF VVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPA LFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGL LSPILNTGPPYCDPTLPNSNGSRGDCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFS VATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLI NMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITT
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 9 |
| A1EQU | (~{S})-[(1~{S},2~{R},4~{S},5~{R})-5-ethenyl-1-azabicyclo[2.2.2]octan-2-yl]-[6-m… | C32 H34 N4 O2 | 1 |
Water and common crystallization additives (NA) are not listed.
Optical control of the cardiac rhythm with photoswitchable Na V 1.5 channel blockers. Liu, S., Guan, W., Li, Z. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-70305-6 · 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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