Cryo-EM structure of rat cardiac sodium channel NaV1.5 with batrachotoxin analog BTX-B. Determined by electron microscopy at 3.3 Å resolution. Released 6 Mar 2024.
Explore 8T6L in 3D Show helices and sheets RCSB PDB PDBe
8T6L contains 73 α-helices and 26 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 |
|---|---|---|---|
| β-strand | 15 | 1 | 1 |
| α-helix | 18-31 | 14 | |
| α-helix | 57-59 | 3 | |
| β-strand | 63-64 | 2 | 2 |
| α-helix | 65-66 | 2 | |
| α-helix | 67-69 | 3 | |
| α-helix | 71-73 | 3 | |
| β-strand | 81-82 | 2 | 1 |
| β-strand | 93-96 | 4 | 1 |
| β-strand | 102-103 | 2 | 2 |
| β-strand | 104-107 | 4 | 1 |
| β-strand | 111 | 1 | 3 |
| β-strand | 115 | 1 | 3 |
| α-helix | 120-130 | 11 | |
| α-helix | 132-148 | 17 | |
| α-helix | 156-158 | 3 | |
| α-helix | 159-180 | 22 | |
| α-helix | 189-191 | 3 | |
| α-helix | 195-209 | 15 | |
| α-helix | 217-228 | 12 | |
| α-helix | 229-233 | 5 | |
| α-helix | 235-249 | 15 | |
| α-helix | 252-272 | 21 | |
| α-helix | 276-278 | 3 | |
| β-strand | 280-283 | 4 | 4 |
| α-helix | 284 | 1 | |
| β-strand | 286-287 | 2 | 5 |
| α-helix | 288 | 1 | |
| β-strand | 295-296 | 2 | 5 |
| β-strand | 301-302 | 2 | 5 |
| α-helix | 305-310 | 6 | |
| β-strand | 317 | 1 | 6 |
| α-helix | 318 | 1 | |
| β-strand | 324 | 1 | 6 |
| α-helix | 325-326 | 2 | |
| β-strand | 340-343 | 4 | 4 |
| α-helix | 350-352 | 3 | |
| α-helix | 359-371 | 13 | |
| α-helix | 375-385 | 11 | |
| α-helix | 388-390 | 3 | |
| α-helix | 391-396 | 6 | |
| α-helix | 397-403 | 7 | |
| α-helix | 404-434 | 31 | |
| α-helix | 701-716 | 16 | |
| α-helix | 718-734 | 17 | |
| β-strand | 739 | 1 | 7 |
| α-helix | 744-771 | 28 | |
| α-helix | 774-778 | 5 | |
| α-helix | 781-799 | 19 | |
| α-helix | 808-821 | 14 | |
| α-helix | 824-837 | 14 | |
| α-helix | 841-861 | 21 | |
| α-helix | 863-868 | 6 | |
| α-helix | 870-872 | 3 | |
| α-helix | 887-898 | 12 | |
| α-helix | 903-910 | 8 | |
| α-helix | 915-943 | 29 | |
| α-helix | 1191-1205 | 15 | |
| α-helix | 1207-1224 | 18 | |
| α-helix | 1235-1262 | 28 | |
| α-helix | 1265-1269 | 5 | |
| α-helix | 1272-1292 | 21 | |
| α-helix | 1299-1306 | 8 | |
| α-helix | 1307-1315 | 9 | |
| α-helix | 1320-1331 | 12 | |
| α-helix | 1333-1357 | 25 | |
| β-strand | 1363-1367 | 5 | 8 |
| β-strand | 1371-1374 | 4 | 8 |
| α-helix | 1375-1376 | 2 | |
| β-strand | 1382 | 1 | 9 |
| α-helix | 1383-1388 | 6 | |
| β-strand | 1395-1399 | 5 | 8 |
| β-strand | 1406 | 1 | 7 |
| α-helix | 1407-1419 | 13 | |
| α-helix | 1424-1430 | 7 | |
| β-strand | 1438 | 1 | 9 |
| α-helix | 1446-1448 | 3 | |
| α-helix | 1449-1455 | 7 | |
| α-helix | 1456-1462 | 7 | |
| α-helix | 1463-1481 | 19 | |
| α-helix | 1491-1503 | 13 | |
| α-helix | 1508-1515 | 8 | |
| α-helix | 1519-1528 | 10 | |
| α-helix | 1530-1548 | 19 | |
| α-helix | 1556-1584 | 29 | |
| α-helix | 1593-1616 | 24 | |
| α-helix | 1618-1620 | 3 | |
| α-helix | 1623-1629 | 7 | |
| α-helix | 1632-1635 | 4 | |
| α-helix | 1636-1639 | 4 | |
| α-helix | 1643-1680 | 38 | |
| α-helix | 1684-1686 | 3 | |
| β-strand | 1687 | 1 | 10 |
| β-strand | 1690 | 1 | 10 |
| α-helix | 1699-1710 | 12 | |
| α-helix | 1715-1723 | 9 | |
| β-strand | 1735 | 1 | 11 |
| β-strand | 1741 | 1 | 11 |
| α-helix | 1747-1779 | 33 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 5 subunit alpha,Green fluorescent protein | A | protein | 1874 | Rattus norvegicus, Aequorea victoria | P15389 (AlphaFold model), P42212 (AlphaFold model) |
>8T6L_1 Sodium channel protein type 5 subunit alpha,Green fluorescent protein (chains A) MANLLLPRGTSSFRRFTRESLAAIEKRMAEKQTRGGSATSQESREGLQEEEAPRPQLDLQ ASKKLPDLYGNPPRELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHP VRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILAR GFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLDNVSALRTFRVLRALKTISVISGLKTI VGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGL VWNSLDVYLNDPANYLLKNGTTDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFA WAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQ NQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSRQRALSAVSVLTSALEELE ESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFADLTITMCIVLNTLFMALE HYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELG LSRMGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVG MQLFGKNYSELRHRISDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLC LLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMNNLQLALARIQRGLRFVKR TTWDFCCGILRRRPKKPAALATHSQLPSCITAPRSPPPPEVEKVPPARKETRFEEDKRPG QGTPGDSEPVCVPIAVAESDTEDQEEDEENSGKVWWRLRKTCYRIVEHSWFETFIIFMIL LSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDF LIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMN VLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWT KVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEDNLYMYIYFVVFIIF GSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNK YQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECI VKMAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRL IRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQT FANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYI IISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSD FADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQME EKFMAANPSKISYEPITTTLRRKHEEVSATVIQRAFRRHLLQRSVKHASFLFRVDLEVLF QGPGSMVSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLP VPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKF EGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQKNGIKVNFKIRHNIEDG SVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKDPNEKRDHMVLLEFVTAAGITLGMD ELYKGSDYKDDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| YIJ | (1R)-1-[(5aR,7aR,9R,11aS,11bS,12R,13aR)-9,12-dihydroxy-2,11a-dimethyl-1,2,3,4,7… | C31 H39 N O6 | 2 |
| 9Z9 | (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en | C34 H56 O5 | 2 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 11 |
| LBN | 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine | C42 H82 N O8 P | 10 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Dual receptor-sites reveal the structural basis for hyperactivation of sodium channels by poison-dart toxin batrachotoxin. Tonggu, L., Wisedchaisri, G., Gamal El-Din, T.M. et al. Nat Commun (2024) 15:2306-2306. DOI 10.1038/s41467-024-45958-w · PubMed
Other PDB entries of the same protein (UniProt P15389 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8T6L directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.