Cryo-EM structure of human Nav1.6 in complex with Iota-Conotoxin RXIA. Determined by electron microscopy at 2.5 Å resolution. Released 20 May 2026.
Explore 25II in 3D Show helices and sheets RCSB PDB PDBe
25II contains 78 α-helices and 37 β-strands across 3 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 |
|---|---|---|---|
| β-strand | 16 | 1 | 1 |
| α-helix | 19-34 | 16 | |
| β-strand | 64 | 1 | 2 |
| α-helix | 71-73 | 3 | |
| β-strand | 80-82 | 3 | 1 |
| β-strand | 93-97 | 5 | 1 |
| β-strand | 102 | 1 | 2 |
| β-strand | 103-107 | 5 | 1 |
| β-strand | 112 | 1 | 3 |
| β-strand | 115 | 1 | 3 |
| α-helix | 120-130 | 11 | |
| α-helix | 132-149 | 18 | |
| α-helix | 156-158 | 3 | |
| α-helix | 159-179 | 21 | |
| α-helix | 189-191 | 3 | |
| α-helix | 193-211 | 19 | |
| α-helix | 217-222 | 6 | |
| α-helix | 223-228 | 6 | |
| α-helix | 229-233 | 5 | |
| α-helix | 237-246 | 10 | |
| α-helix | 249-251 | 3 | |
| α-helix | 252-272 | 21 | |
| α-helix | 276-278 | 3 | |
| β-strand | 279-283 | 5 | 4 |
| α-helix | 288-290 | 3 | |
| β-strand | 292 | 1 | 5 |
| β-strand | 298 | 1 | 5 |
| α-helix | 302-305 | 4 | |
| α-helix | 309-311 | 3 | |
| β-strand | 312 | 1 | 4 |
| α-helix | 321-323 | 3 | |
| α-helix | 333-334 | 2 | |
| β-strand | 337-341 | 5 | 4 |
| α-helix | 356-368 | 13 | |
| α-helix | 372-383 | 12 | |
| α-helix | 385-387 | 3 | |
| α-helix | 388-394 | 7 | |
| α-helix | 395-402 | 8 | |
| α-helix | 403-435 | 33 | |
| α-helix | 739-750 | 12 | |
| α-helix | 753-770 | 18 | |
| α-helix | 779-806 | 28 | |
| α-helix | 817-832 | 16 | |
| α-helix | 840-844 | 5 | |
| α-helix | 845-856 | 12 | |
| α-helix | 859-871 | 13 | |
| α-helix | 876-903 | 28 | |
| α-helix | 905-908 | 4 | |
| α-helix | 922-934 | 13 | |
| α-helix | 938-947 | 10 | |
| α-helix | 950-980 | 31 | |
| α-helix | 997-1006 | 10 | |
| α-helix | 1180-1196 | 17 | |
| α-helix | 1198-1213 | 16 | |
| α-helix | 1214-1217 | 4 | |
| α-helix | 1220-1224 | 5 | |
| α-helix | 1226-1254 | 29 | |
| α-helix | 1256-1260 | 5 | |
| α-helix | 1263-1283 | 21 | |
| α-helix | 1286-1288 | 3 | |
| α-helix | 1290-1296 | 7 | |
| α-helix | 1297-1305 | 9 | |
| α-helix | 1306-1309 | 4 | |
| α-helix | 1311-1349 | 39 | |
| β-strand | 1354-1358 | 5 | 6 |
| β-strand | 1363-1364 | 2 | 6 |
| α-helix | 1365-1366 | 2 | |
| β-strand | 1372 | 1 | 7 |
| α-helix | 1373-1380 | 8 | |
| β-strand | 1387-1391 | 5 | 6 |
| α-helix | 1399-1411 | 13 | |
| α-helix | 1415-1422 | 8 | |
| β-strand | 1430 | 1 | 7 |
| α-helix | 1438-1440 | 3 | |
| α-helix | 1441-1447 | 7 | |
| α-helix | 1448-1454 | 7 | |
| α-helix | 1455-1469 | 15 | |
| α-helix | 1483-1494 | 12 | |
| α-helix | 1514-1520 | 7 | |
| α-helix | 1522-1539 | 18 | |
| α-helix | 1548-1575 | 28 | |
| α-helix | 1585-1601 | 17 | |
| α-helix | 1603-1606 | 4 | |
| α-helix | 1613-1619 | 7 | |
| α-helix | 1620-1632 | 13 | |
| α-helix | 1635-1646 | 12 | |
| α-helix | 1648-1672 | 25 | |
| α-helix | 1691-1701 | 11 | |
| α-helix | 1707-1711 | 5 | |
| α-helix | 1713-1715 | 3 | |
| β-strand | 1726 | 1 | 8 |
| β-strand | 1733 | 1 | 8 |
| α-helix | 1739-1771 | 33 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-27 | 3 | |
| β-strand | 29-31 | 3 | 9 |
| β-strand | 36-38 | 3 | 10 |
| β-strand | 41 | 1 | 11 |
| β-strand | 50-61 | 12 | 12 |
| β-strand | 68-74 | 7 | 12 |
| β-strand | 77-80 | 4 | 12 |
| α-helix | 84-86 | 3 | |
| β-strand | 90-92 | 3 | 10 |
| β-strand | 103 | 1 | 11 |
| β-strand | 106-108 | 3 | 10 |
| α-helix | 113-115 | 3 | |
| β-strand | 117-129 | 13 | 12 |
| β-strand | 132-144 | 13 | 12 |
| β-strand | 145-147 | 3 | 9 |
| α-helix | 154-190 | 37 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6 | 1 | 13 |
| β-strand | 11 | 1 | 14 |
| α-helix | 15-17 | 3 | |
| β-strand | 18 | 1 | 13 |
| β-strand | 21-23 | 3 | 14 |
| β-strand | 26-28 | 3 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 8 subunit alpha | A | protein | 1980 | Homo sapiens | Q9UQD0 (AlphaFold model) |
| Sodium channel regulatory subunit beta-1 | C | protein | 218 | Homo sapiens | Q07699 (AlphaFold model) |
| Iota-conotoxin RXIA | D | protein | 46 | Conus radiatus | Q7Z094 (AlphaFold model) |
>25II_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
>25II_2 Sodium channel regulatory subunit beta-1 (chains C) MGRLLALVVGAALVSSACGGCVEVDSETEAVYGMTFKILCISCKRRSETNAETFTEWTFR QKGTEEFVKILRYENEVLQLEEDERFEGRVVWNGSRGTKDLQDLSIFITNVTYNHSGDYE CHVYRLLFFENYEHNTSVVKKIHIEVVDKANRDMASIVSEIMMYVLIVVLTIWLVAEMIY CYKKIAAATETAAQENASEYLAITSESKENCTGVQVAE
>25II_3 Iota-conotoxin RXIA (chains D) GPSFCKADEKPCEYHADCCNCCLSGICAPSTNWILPGCSTSSFFKI
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 7 |
| 9Z9 | (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en | C34 H56 O5 | 1 |
| PCW | 1,2-dioleoyl-sn-glycero-3-phosphocholine | C44 H85 N O8 P | 5 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 3 |
| CLR | Cholesterol | C27 H46 O | 1 |
| P5S | O-[(R)-{[(2R)-2,3-bis(octadecanoyloxy)propyl]oxy}(hydroxy)phosphoryl]-L-serine | C42 H82 N O10 P | 1 |
| LPE | 1-O-octadecyl-sn-glycero-3-phosphocholine | C26 H57 N O6 P | 1 |
| P3X | (5E,17R,20S)-23-amino-20-hydroxy-14,20-dioxo-15,19,21-trioxa-20lambda~5~-phosph… | C35 H68 N O8 P | 1 |
Water and common crystallization additives (NA) are not listed.
Diverse binding poses of agonistic neurotoxins on human Na v 1.6. Fan, X., Huang, J., Yang, L. et al. Nature (2026) 656:250-259. DOI 10.1038/s41586-026-10661-x · 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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