Cryo-EM structure of a human-cockroach hybrid Nav channel bound to alpha-scorpion toxin AaH2. Determined by electron microscopy at 3.5 Å resolution. Released 20 Feb 2019.
Explore 6NT4 in 3D Show helices and sheets RCSB PDB PDBe
6NT4 contains 78 α-helices and 21 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 |
|---|---|---|---|
| α-helix | 54 | 1 | |
| α-helix | 55-59 | 5 | |
| β-strand | 76 | 1 | 1 |
| β-strand | 81 | 1 | 1 |
| α-helix | 100-109 | 10 | |
| α-helix | 130-137 | 8 | |
| α-helix | 140-157 | 18 | |
| α-helix | 166-187 | 22 | |
| α-helix | 192-196 | 5 | |
| α-helix | 200-214 | 15 | |
| α-helix | 228-239 | 12 | |
| α-helix | 245-275 | 31 | |
| β-strand | 287-290 | 4 | 2 |
| α-helix | 305-310 | 6 | |
| α-helix | 337-338 | 2 | |
| β-strand | 341-344 | 4 | 2 |
| α-helix | 352-354 | 3 | |
| α-helix | 361-372 | 12 | |
| α-helix | 377-388 | 12 | |
| α-helix | 390-392 | 3 | |
| α-helix | 393-401 | 9 | |
| α-helix | 404-408 | 5 | |
| α-helix | 409-432 | 24 | |
| α-helix | 503-516 | 14 | |
| α-helix | 522-536 | 15 | |
| α-helix | 545-572 | 28 | |
| α-helix | 578-581 | 4 | |
| α-helix | 584-603 | 20 | |
| α-helix | 609-613 | 5 | |
| α-helix | 614-622 | 9 | |
| α-helix | 625-636 | 12 | |
| α-helix | 639-662 | 24 | |
| α-helix | 666-669 | 4 | |
| α-helix | 687-699 | 13 | |
| α-helix | 703-711 | 9 | |
| α-helix | 718-727 | 10 | |
| α-helix | 728-732 | 5 | |
| α-helix | 733-740 | 8 | |
| α-helix | 839-852 | 14 | |
| α-helix | 856-870 | 15 | |
| α-helix | 871-873 | 3 | |
| α-helix | 886-912 | 27 | |
| α-helix | 914-917 | 4 | |
| α-helix | 923-942 | 20 | |
| α-helix | 945-946 | 2 | |
| α-helix | 948-950 | 3 | |
| α-helix | 955-958 | 4 | |
| α-helix | 959-962 | 4 | |
| α-helix | 966-968 | 3 | |
| α-helix | 969-1003 | 35 | |
| β-strand | 1010 | 1 | 3 |
| β-strand | 1012 | 1 | 4 |
| β-strand | 1018 | 1 | 4 |
| α-helix | 1027-1032 | 6 | |
| β-strand | 1038 | 1 | 3 |
| α-helix | 1039-1040 | 2 | |
| α-helix | 1048-1058 | 11 | |
| α-helix | 1064-1072 | 9 | |
| α-helix | 1089-1100 | 12 | |
| α-helix | 1104-1107 | 4 | |
| α-helix | 1109-1123 | 15 | |
| α-helix | 1133-1140 | 8 | |
| α-helix | 1141-1144 | 4 | |
| α-helix | 1160-1164 | 5 | |
| α-helix | 1170-1173 | 4 | |
| α-helix | 1177-1185 | 9 | |
| α-helix | 1186-1189 | 4 | |
| α-helix | 1198-1223 | 26 | |
| α-helix | 1232-1246 | 15 | |
| α-helix | 1261-1272 | 12 | |
| α-helix | 1274-1277 | 4 | |
| α-helix | 1291-1294 | 4 | |
| α-helix | 1296-1320 | 25 | |
| α-helix | 1340-1349 | 10 | |
| α-helix | 1355-1362 | 8 | |
| β-strand | 1372 | 1 | 5 |
| β-strand | 1377 | 1 | 5 |
| α-helix | 1385-1389 | 5 | |
| α-helix | 1394-1397 | 4 | |
| α-helix | 1398-1402 | 5 | |
| α-helix | 1403-1423 | 21 | |
| α-helix | 1427-1439 | 13 | |
| β-strand | 1447 | 1 | 6 |
| α-helix | 1451-1456 | 6 | |
| α-helix | 1473-1476 | 4 | |
| β-strand | 1488 | 1 | 6 |
| α-helix | 1489-1503 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 19-27 | 9 | |
| β-strand | 34-37 | 4 | 7 |
| β-strand | 45-48 | 4 | 7 |
| α-helix | 56-57 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-4 | 3 | 8 |
| β-strand | 6 | 1 | 9 |
| β-strand | 7 | 1 | 10 |
| β-strand | 13 | 1 | 10 |
| α-helix | 20-27 | 8 | |
| β-strand | 33-37 | 5 | 8 |
| β-strand | 45-51 | 7 | 8 |
| β-strand | 57 | 1 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein PaFPC1,Sodium channel protein type 9 subunit alpha,Sodium channel protein… | A | protein | 1559 | Periplaneta americana, Homo sapiens | D0E0C2 (AlphaFold model), Q15858 (AlphaFold model) |
| Alpha-mammal toxin AaH2 | B, C | protein | 65 | Androctonus australis | P01484 (AlphaFold model) |
>6NT4_1 Sodium channel protein PaFPC1,Sodium channel protein type 9 subunit alpha,Sodium channel protein PaFPC1 (chains A) WSHPQFEKGGGSGGGSGGSAWSHPQFEKGGSGGDYKDDDDKGGSGGDYKDDDDKMADNSP LIREERQRLFRPYTRAMLTAPSAQPAKENGKTEENKDNSRDKGRGANKDRDGSAHPDQAL EQGSRLPARMRNIFPAELASTPLEDFDPFYKNKKTFVVVTKAGDIFRFSGEKSLWMLDPF TPIRRVAISTMVQPIFSYFIMITILIHCIFMIMPATQTTYILELVFLSIYTIEVVVKVLA RGFILHPFAYLRDPWNWLDFLVTLIGYITLVVDLGHLYALRAFRVLRSWRTVTIVPGWRT IVDALSLSITSLKDLVLLLLFSLSVFALIGLQLFMGNLKHKCVKHFPADGSWGNFTDERW FNYTSNSSHWYIPDDWIEYPLCGNSSGAGMCPPGYTCLQGYGGNPNYGYTSFDTFGWAFL SVFRLVTLDYWEDLYQLALRSAGPWHILFFIIVVFYGTFCFLNFILAVVVMSYTHMVKRA DEEKAAERELKKEKKAASVANNTANGQEQTTIEMNGDEAVVIDNNDQAARQQSDPETPAP SVTQRLTDFLCVWDCCVPWQKLQGAIGAVVLSPFFELFIAVIIVLNITFMALDHHDMNIE FERILRTGNYIFTSIYIVEAVLKIIALSPKFYFKDSWNVFDFIIVVFAILELGLEGVQGL SVFRSFRLLRVFRLAKFWPTLNNFMSVMTKSYGAFVNVMYVMFLLLFIFAIIGMQLFGMN YIDNMERFPDGDLPRWNFTDFLHSFMIVFRALCGEWIESMWDCMLVGDWSCIPFFVAVFF VGNLVILNLLIALLLNNYGSFCTSPTSDEEDSKDEDALAQIVRIFKRFKPNLNAVKLSPM KPDSEDIVESQEIQGNNIADAEDVLAGEFPPDCCCNAFYKCFPSRPARDSSVQRMWSNIR RVCFLLAKNKYFQKFVTAVLVITSVLLALEDIYLPQRPVLVNITLYVDYVLTAFFVIEMI IMLFAVGFKKYFTSKWYWLDFIVVVAYLLNFVLMCAGIEALQTLRLLRVFRLFRPLSKVN GMQVVTSTLVEAVPHIFNVILVGIFFWLVFAIMGVQLFAGKFYKCVDENSTVLSHEITMD RNDCLHENYTWENSPMNFDHVGNAYLSLLQVATFKGWLQIMNDAIDSREVHKQPIRETNI YMYLYFIFFIVFGSFFILKLFVCILIDIFRQQRRKAEGLSATDSRTQLIYRRAVMRTMSA KPVKRIPKPGNKIQGCIFDLVTNQAFDISIMVLICLNMVTMMVEKEGQSQHMTEVLYWIN VVFIILFTGECVLKLISLRHYYFTVGWNIFDFVVVIISIVGMFLADLIETYFVSPTLFRV IRLARIGRILRLVKGAKGIRLLLLALRKALRTLFNVSFLLFVIMFVYAVFGMEFFMHIRD AGAIDDVYNFKTFGQSIILLFQLATSAGWDGVYFAIANEEDCRAPDHELGYPGNCGSRAL GIAYLVSYLIITCLVVINMYAAVILDYVLEVYEDSKEGLTDDDYDMFFEVWQQFDPEATQ YIRYDQLSELLEALQPPLQVQKPNKYKILSMNIPICKDDHIFYKDVLEALVKDVFSRRG
>6NT4_2 Alpha-mammal toxin AaH2 (chains B, C) VKDGYIVDDVNCTYFCGRNAYCNEECTKLKGESGYCQWASPYGNACYCYKLPDHVRTKGP GRCHX
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 5 |
| 76F | (7E,21R,24S)-27-amino-24-hydroxy-18,24-dioxo-19,23,25-trioxa-24lambda~5~-phosph… | C41 H76 N O8 P | 5 |
| AJP | Digitonin | C56 H92 O29 | 1 |
| LHG | 1,2-dipalmitoyl-phosphatidyl-glycerole | C38 H75 O10 P | 1 |
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 1 |
Structural basis of alpha-scorpion toxin action on Na v channels. Clairfeuille, T., Cloake, A., Infield, D.T. et al. Science (2019) 363. DOI 10.1126/science.aav8573 · PubMed
Other PDB entries of the same protein (UniProt D0E0C2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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