Cryo-EM structure of human voltage-gated sodium channel Nav1.6. Determined by electron microscopy at 3.1 Å resolution. Released 8 Feb 2023.
Explore 8FHD in 3D Show helices and sheets RCSB PDB PDBe
8FHD contains 69 α-helices and 25 β-strands across 2 chains. 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 | 19-34 | 16 | |
| α-helix | 64-66 | 3 | |
| α-helix | 67-69 | 3 | |
| β-strand | 81 | 1 | 1 |
| β-strand | 94-97 | 4 | 1 |
| β-strand | 103-106 | 4 | 1 |
| α-helix | 110 | 1 | |
| β-strand | 111 | 1 | 2 |
| β-strand | 115 | 1 | 2 |
| α-helix | 117-119 | 3 | |
| α-helix | 122-129 | 8 | |
| α-helix | 132-150 | 19 | |
| α-helix | 156-158 | 3 | |
| α-helix | 159-179 | 21 | |
| β-strand | 182 | 1 | 3 |
| β-strand | 189 | 1 | 3 |
| α-helix | 193-207 | 15 | |
| α-helix | 216-223 | 8 | |
| α-helix | 224-228 | 5 | |
| α-helix | 229-233 | 5 | |
| α-helix | 237-249 | 13 | |
| α-helix | 253-272 | 20 | |
| β-strand | 279-283 | 5 | 4 |
| α-helix | 288-290 | 3 | |
| α-helix | 321-322 | 2 | |
| β-strand | 323 | 1 | 4 |
| β-strand | 337-341 | 5 | 4 |
| α-helix | 356-367 | 12 | |
| α-helix | 372-383 | 12 | |
| α-helix | 385-387 | 3 | |
| α-helix | 388-396 | 9 | |
| α-helix | 401-443 | 43 | |
| α-helix | 739-747 | 9 | |
| α-helix | 753-770 | 18 | |
| α-helix | 779-806 | 28 | |
| α-helix | 820-832 | 13 | |
| α-helix | 840-843 | 4 | |
| α-helix | 847-856 | 10 | |
| α-helix | 859-871 | 13 | |
| α-helix | 876-897 | 22 | |
| α-helix | 900-903 | 4 | |
| α-helix | 905-907 | 3 | |
| α-helix | 922-934 | 13 | |
| α-helix | 938-948 | 11 | |
| α-helix | 951-979 | 29 | |
| α-helix | 981-983 | 3 | |
| α-helix | 996-1006 | 11 | |
| α-helix | 1179-1196 | 18 | |
| α-helix | 1200-1214 | 15 | |
| α-helix | 1220-1223 | 4 | |
| α-helix | 1226-1254 | 29 | |
| α-helix | 1256-1260 | 5 | |
| α-helix | 1263-1284 | 22 | |
| α-helix | 1290-1296 | 7 | |
| α-helix | 1297-1301 | 5 | |
| α-helix | 1311-1346 | 36 | |
| β-strand | 1354-1358 | 5 | 5 |
| β-strand | 1363-1364 | 2 | 5 |
| α-helix | 1365-1366 | 2 | |
| α-helix | 1373-1379 | 7 | |
| β-strand | 1387-1391 | 5 | 5 |
| α-helix | 1399-1410 | 12 | |
| α-helix | 1415-1424 | 10 | |
| α-helix | 1438-1440 | 3 | |
| α-helix | 1441-1449 | 9 | |
| α-helix | 1450-1454 | 5 | |
| α-helix | 1455-1474 | 20 | |
| α-helix | 1483-1496 | 14 | |
| α-helix | 1498-1500 | 3 | |
| α-helix | 1514-1519 | 6 | |
| α-helix | 1522-1538 | 17 | |
| α-helix | 1548-1572 | 25 | |
| α-helix | 1585-1597 | 13 | |
| α-helix | 1598-1602 | 5 | |
| α-helix | 1603-1605 | 3 | |
| α-helix | 1615-1620 | 6 | |
| α-helix | 1621-1631 | 11 | |
| α-helix | 1635-1672 | 38 | |
| α-helix | 1691-1702 | 12 | |
| α-helix | 1739-1772 | 34 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-31 | 3 | 6 |
| β-strand | 38 | 1 | 7 |
| β-strand | 41 | 1 | 8 |
| β-strand | 51-61 | 11 | 9 |
| β-strand | 68-74 | 7 | 9 |
| β-strand | 77-80 | 4 | 9 |
| β-strand | 91-92 | 2 | 7 |
| β-strand | 103 | 1 | 8 |
| β-strand | 106-107 | 2 | 7 |
| β-strand | 117-129 | 13 | 9 |
| β-strand | 132-143 | 12 | 9 |
| β-strand | 145-147 | 3 | 6 |
| α-helix | 150-153 | 4 | |
| α-helix | 154-191 | 38 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 8 subunit alpha | A | protein | 1980 | Homo sapiens | Q9UQD0 (AlphaFold model) |
| Sodium channel subunit beta-1 | C | protein | 218 | Homo sapiens | Q07699 (AlphaFold model) |
>8FHD_1 Sodium channel protein type 8 subunit alpha (chains A) MAARLLAPPGPDSFKPFTPESLANIERRIAESKLKKPPKADGSHREDDEDSKPKPNSDLE AGKSLPFIYGDIPQGLVAVPLEDFDPYYLTQKTFVVLNRGKTLFRFSATPALYILSPFNL IRRIAIKILIHSVFSMIIMCTILTNCVFMTFSNPPDWSKNVEYTFTGIYTFESLVKIIAR GFCIDGFTFLRDPWNWLDFSVIMMAYITEFVNLGNVSALRTFRVLRALKTISVIPGLKTI VGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVVWPINFNESYLENGTKGF DWEEYINNKTNFYTVPGMLEPLLCGNSSDAGQCPEGYQCMKAGRNPNYGYTSFDTFSWAF LALFRLMTQDYWENLYQLTLRAAGKTYMIFFVLVIFVGSFYLVNLILAVVAMAYEEQNQA TLEEAEQKEAEFKAMLEQLKKQQEEAQAAAMATSAGTVSEDAIEEEGEEGGGSPRSSSEI SKLSSKSAKERRNRRKKRKQKELSEGEEKGDPEKVFKSESEDGMRRKAFRLPDNRIGRKF SIMNQSLLSIPGSPFLSRHNSKSSIFSFRGPGRFRDPGSENEFADDEHSTVEESEGRRDS LFIPIRARERRSSYSGYSGYSQGSRSSRIFPSLRRSVKRNSTVDCNGVVSLIGGPGSHIG GRLLPEATTEVEIKKKGPGSLLVSMDQLASYGRKDRINSIMSVVTNTLVEELEESQRKCP PCWYKFANTFLIWECHPYWIKLKEIVNLIVMDPFVDLAITICIVLNTLFMAMEHHPMTPQ FEHVLAVGNLVFTGIFTAEMFLKLIAMDPYYYFQEGWNIFDGFIVSLSLMELSLADVEGL SVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKS YKECVCKINQDCELPRWHMHDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVFMMV MVIGNLVVLNLFLALLLSSFSADNLAATDDDGEMNNLQISVIRIKKGVAWTKLKVHAFMQ AHFKQREADEVKPLDELYEKKANCIANHTGADIHRNGDFQKNGNGTTSGIGSSVEKYIID EDHMSFINNPNLTVRVPIAVGESDFENLNTEDVSSESDPEGSKDKLDDTSSSEGSTIDIK PEVEEVPVEQPEEYLDPDACFTEGCVQRFKCCQVNIEEGLGKSWWILRKTCFLIVEHNWF ETFIIFMILLSSGALAFEDIYIEQRKTIRTILEYADKVFTYIFILEMLLKWTAYGFVKFF TNAWCWLDFLIVAVSLVSLIANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNAL VGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKYHYCFNETSEIRFEIEDVNNKTECEKLM EGNNTEIRWKNVKINFDNVGAGYLALLQVATFKGWMDIMYAAVDSRKPDEQPKYEDNIYM YIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKP QKPIPRPLNKIQGIVFDFVTQQAFDIVIMMLICLNMVTMMVETDTQSKQMENILYWINLV FVIFFTCECVLKMFALRHYYFTIGWNIFDFVVVILSIVGMFLADIIEKYFVSPTLFRVIR LARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIFSIFGMSNFAYVKHEA GIDDMFNFETFGNSMICLFQITTSAGWDGLLLPILNRPPDCSLDKEHPGSGFKGDCGNPS VGIFFFVSYIIISFLIVVNMYIAIILENFSVATEESADPLSEDDFETFYEIWEKFDPDAT QFIEYCKLADFADALEHPLRVPKPNTIELIAMDLPMVSGDRIHCLDILFAFTKRVLGDSG ELDILRQQMEERFVASNPSKVSYEPITTTLRRKQEEVSAVVLQRAYRGHLARRGFICKKT TSNKLENGGTHREKKESTPSTASLPSYDSVTKPEKEKQQRAEEGRRERAKRQKEVRESKC
>8FHD_2 Sodium channel subunit beta-1 (chains C) MGRLLALVVGAALVSSACGGCVEVDSETEAVYGMTFKILCISCKRRSETNAETFTEWTFR QKGTEEFVKILRYENEVLQLEEDERFEGRVVWNGSRGTKDLQDLSIFITNVTYNHSGDYE CHVYRLLFFENYEHNTSVVKKIHIEVVDKANRDMASIVSEIMMYVLIVVLTIWLVAEMIY CYKKIAAATETAAQENASEYLAITSESKENCTGVQVAE
| ID | Name | Formula | Copies |
|---|---|---|---|
| LPE | 1-O-octadecyl-sn-glycero-3-phosphocholine | C26 H57 N O6 P | 5 |
| PCW | 1,2-dioleoyl-sn-glycero-3-phosphocholine | C44 H85 N O8 P | 3 |
| CLR | Cholesterol | C27 H46 O | 1 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 4 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 7 |
| P3X | (5E,17R,20S)-23-amino-20-hydroxy-14,20-dioxo-15,19,21-trioxa-20lambda~5~-phosph… | C35 H68 N O8 P | 1 |
| 9Z9 | (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en | C34 H56 O5 | 1 |
| P5S | O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine | C42 H82 N O10 P | 2 |
Cryo-EM structure of human voltage-gated sodium channel Na v 1.6. Fan, X., Huang, J., Jin, X. et al. Proc Natl Acad Sci U S A (2023) 120:e2220578120-e2220578120. DOI 10.1073/pnas.2220578120 · PubMed
Other PDB entries of the same protein (UniProt Q9UQD0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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