structure of a channel. Determined by electron microscopy at 3.4 Å resolution. Released 22 Sept 2021.
Explore 7FBS in 3D Show helices and sheets RCSB PDB PDBe
7FBS contains 66 α-helices and 12 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 | 120-130 | 11 | |
| α-helix | 132-149 | 18 | |
| α-helix | 156-158 | 3 | |
| α-helix | 159-180 | 22 | |
| α-helix | 183-191 | 9 | |
| α-helix | 194-210 | 17 | |
| α-helix | 219-222 | 4 | |
| α-helix | 225-233 | 9 | |
| α-helix | 235-243 | 9 | |
| α-helix | 246-250 | 5 | |
| α-helix | 252-273 | 22 | |
| β-strand | 280 | 1 | 1 |
| β-strand | 282 | 1 | 2 |
| β-strand | 283 | 1 | 3 |
| α-helix | 304-307 | 4 | |
| β-strand | 315 | 1 | 2 |
| β-strand | 317 | 1 | 4 |
| α-helix | 318 | 1 | |
| β-strand | 324 | 1 | 4 |
| α-helix | 325-326 | 2 | |
| α-helix | 336-337 | 2 | |
| β-strand | 340 | 1 | 3 |
| β-strand | 343 | 1 | 1 |
| α-helix | 359-370 | 12 | |
| α-helix | 375-385 | 11 | |
| α-helix | 388-390 | 3 | |
| α-helix | 391-397 | 7 | |
| α-helix | 398-405 | 8 | |
| α-helix | 406-428 | 23 | |
| α-helix | 705-714 | 10 | |
| α-helix | 721-735 | 15 | |
| α-helix | 744-771 | 28 | |
| α-helix | 774-779 | 6 | |
| α-helix | 781-796 | 16 | |
| α-helix | 807-821 | 15 | |
| α-helix | 824-836 | 13 | |
| α-helix | 841-868 | 28 | |
| α-helix | 869-872 | 4 | |
| α-helix | 887-899 | 13 | |
| α-helix | 903-912 | 10 | |
| α-helix | 915-943 | 29 | |
| α-helix | 1192-1205 | 14 | |
| α-helix | 1207-1224 | 18 | |
| α-helix | 1235-1263 | 29 | |
| α-helix | 1265-1269 | 5 | |
| α-helix | 1272-1292 | 21 | |
| α-helix | 1300-1304 | 5 | |
| α-helix | 1305-1314 | 10 | |
| α-helix | 1315-1318 | 4 | |
| α-helix | 1322-1330 | 9 | |
| α-helix | 1333-1357 | 25 | |
| β-strand | 1366-1367 | 2 | 5 |
| β-strand | 1382 | 1 | 6 |
| α-helix | 1385-1388 | 4 | |
| β-strand | 1395-1396 | 2 | 5 |
| α-helix | 1407-1418 | 12 | |
| α-helix | 1423-1430 | 8 | |
| β-strand | 1438 | 1 | 6 |
| α-helix | 1439-1441 | 3 | |
| α-helix | 1446-1448 | 3 | |
| α-helix | 1449-1455 | 7 | |
| α-helix | 1456-1462 | 7 | |
| α-helix | 1463-1480 | 18 | |
| α-helix | 1491-1502 | 12 | |
| α-helix | 1518-1528 | 11 | |
| α-helix | 1530-1548 | 19 | |
| α-helix | 1556-1581 | 26 | |
| α-helix | 1587-1590 | 4 | |
| α-helix | 1592-1612 | 21 | |
| α-helix | 1623-1627 | 5 | |
| α-helix | 1628-1631 | 4 | |
| α-helix | 1632-1636 | 5 | |
| α-helix | 1637-1640 | 4 | |
| α-helix | 1644-1654 | 11 | |
| α-helix | 1656-1680 | 25 | |
| α-helix | 1699-1710 | 12 | |
| α-helix | 1715-1723 | 9 | |
| α-helix | 1747-1776 | 30 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 5 subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium… | A | protein | 1838 | Rattus norvegicus, Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP | B7UCZ6, P15389 (AlphaFold model) |
>7FBS_1 Sodium channel protein type 5 subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type 5 subunit alpha,G protein/GFP fusion protein (chains A) MANLLLPRGTSSFRRFTRESLAAIEKRMAEKQARGGSATSQESREGLQEEEAPRPQLDLQ ASKKLPDLYGNPPRELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHP VRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILAR GFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTI VGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGL VWNSLDVYLNDPANYLLKNGTTDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFA WAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQ NQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSARQRALSAVSVLTSALEEL EESHRKCPPCWNRFAQHYLIWECCPLWMSIKQKVKFVVMDPFADLTITMCIVLNTLFMAL EHYNMTAEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMEL GLSRMGNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVV GMQLFGKNYSELRHRISDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSL CLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDGEMNNLQLALARIQRGLRFVK RTTWDFCCGILRRRPKKPAALATHSQLPSCITAPRSPPPPEVEKVPPARKETRFEEDKRP GQGTPGDSEPVCVPIAVAESDTEDQEEDEENGKVWWRLRKTCYRIVEHSWFETFIIFMIL LSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDF LIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMN VLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSECESFNVTGELYWT KVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEDNLYMYIYFVVFIIF GSFFTLNLFIGVIIDNFNQQKKKLGGQDQQQTEEQKKYYNAMKKLGSKKPQKPIPRPLNK YQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKVNILAKINLLFVAIFTGECI VKMAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRL IRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQT FANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPNLPNSNGSRGNCGSPAVGILFFTTYI IISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYLALSD FADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQME EKFMAANPSKISYEPITTTLEVLFQGPGSMVSKGEELFTGVVPILVELDGDVNGHKFSVS GEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLTYGVQCFSRYPDHMKQHDFFKSAMPE GYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNV YIMADKQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSALSKD PNEKRDHMVLLEFVTAAGITLGMDELYKGSDYKDDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6OU | [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-y… | C39 H76 N O8 P | 11 |
| 4Y4 | 1-[2-[(2R)-2-oxidanyl-3-(propylamino)propoxy]phenyl]-3-phenyl-propan-1-one | C21 H27 N O3 | 1 |
| 9Z9 | (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en | C34 H56 O5 | 2 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Open-state structure and pore gating mechanism of the cardiac sodium channel. Jiang, D., Banh, R., Gamal El-Din, T.M. et al. Cell (2021) 184:5151. DOI 10.1016/j.cell.2021.08.021 · PubMed
Other PDB entries of the same protein (UniProt B7UCZ6), best resolution first:
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