Complex of voltage-gated sodium channel NavPaS from American cockroach Periplaneta americana bound with tetrodotoxin and Dc1a. Determined by electron microscopy at 2.6 Å resolution. Released 8 Aug 2018.
Explore 6A95 in 3D Show helices and sheets RCSB PDB PDBe
6A95 contains 87 α-helices and 22 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 | 52-55 | 4 | |
| α-helix | 128-137 | 10 | |
| α-helix | 140-153 | 14 | |
| α-helix | 155-158 | 4 | |
| α-helix | 160-161 | 2 | |
| α-helix | 163-185 | 23 | |
| α-helix | 203-214 | 12 | |
| α-helix | 226-240 | 15 | |
| α-helix | 244-256 | 13 | |
| α-helix | 259-280 | 22 | |
| α-helix | 283-285 | 3 | |
| β-strand | 286-287 | 2 | 1 |
| β-strand | 289 | 1 | 2 |
| β-strand | 290 | 1 | 3 |
| α-helix | 291-293 | 3 | |
| α-helix | 303-310 | 8 | |
| α-helix | 313-315 | 3 | |
| β-strand | 316 | 1 | 2 |
| α-helix | 325-326 | 2 | |
| β-strand | 327 | 1 | 1 |
| β-strand | 341 | 1 | 3 |
| β-strand | 344-345 | 2 | 1 |
| α-helix | 361-372 | 12 | |
| α-helix | 377-387 | 11 | |
| α-helix | 390-392 | 3 | |
| α-helix | 393-402 | 10 | |
| α-helix | 403-407 | 5 | |
| α-helix | 408-434 | 27 | |
| α-helix | 511-516 | 6 | |
| α-helix | 519-537 | 19 | |
| β-strand | 543 | 1 | 4 |
| α-helix | 546-568 | 23 | |
| α-helix | 578-580 | 3 | |
| α-helix | 584-599 | 16 | |
| α-helix | 609-622 | 14 | |
| α-helix | 625-634 | 10 | |
| α-helix | 638-663 | 26 | |
| α-helix | 666-669 | 4 | |
| α-helix | 671-673 | 3 | |
| α-helix | 675-677 | 3 | |
| α-helix | 687-698 | 12 | |
| α-helix | 703-712 | 10 | |
| α-helix | 715-717 | 3 | |
| α-helix | 718-725 | 8 | |
| α-helix | 726-732 | 7 | |
| α-helix | 733-741 | 9 | |
| α-helix | 841-854 | 14 | |
| α-helix | 856-874 | 19 | |
| α-helix | 880-882 | 3 | |
| α-helix | 884-911 | 28 | |
| α-helix | 921-940 | 20 | |
| α-helix | 945-947 | 3 | |
| α-helix | 948-951 | 4 | |
| α-helix | 952-959 | 8 | |
| α-helix | 962-964 | 3 | |
| α-helix | 968-976 | 9 | |
| α-helix | 979-1004 | 26 | |
| β-strand | 1009-1012 | 4 | 5 |
| α-helix | 1017 | 1 | |
| β-strand | 1018 | 1 | 5 |
| α-helix | 1019-1020 | 2 | |
| β-strand | 1026 | 1 | 6 |
| α-helix | 1027-1032 | 6 | |
| β-strand | 1036-1039 | 4 | 5 |
| α-helix | 1047-1058 | 12 | |
| α-helix | 1063-1072 | 10 | |
| β-strand | 1078 | 1 | 6 |
| α-helix | 1086-1088 | 3 | |
| α-helix | 1089-1095 | 7 | |
| α-helix | 1096-1104 | 9 | |
| α-helix | 1106-1122 | 17 | |
| α-helix | 1131-1143 | 13 | |
| α-helix | 1148-1154 | 7 | |
| α-helix | 1158-1165 | 8 | |
| α-helix | 1170-1185 | 16 | |
| α-helix | 1187-1189 | 3 | |
| α-helix | 1196-1204 | 9 | |
| α-helix | 1207-1222 | 16 | |
| α-helix | 1226-1230 | 5 | |
| α-helix | 1232-1248 | 17 | |
| α-helix | 1261-1270 | 10 | |
| α-helix | 1271-1274 | 4 | |
| α-helix | 1275-1278 | 4 | |
| α-helix | 1283-1294 | 12 | |
| α-helix | 1296-1320 | 25 | |
| α-helix | 1339-1348 | 10 | |
| α-helix | 1349-1351 | 3 | |
| α-helix | 1355-1362 | 8 | |
| α-helix | 1369-1371 | 3 | |
| β-strand | 1372 | 1 | 7 |
| β-strand | 1377 | 1 | 7 |
| α-helix | 1384-1394 | 11 | |
| α-helix | 1395-1402 | 8 | |
| α-helix | 1404-1422 | 19 | |
| α-helix | 1428-1436 | 9 | |
| β-strand | 1447-1449 | 3 | 8 |
| α-helix | 1450-1452 | 3 | |
| α-helix | 1453-1458 | 6 | |
| α-helix | 1465-1467 | 3 | |
| α-helix | 1470-1474 | 5 | |
| α-helix | 1483-1485 | 3 | |
| β-strand | 1486-1488 | 3 | 8 |
| α-helix | 1489-1503 | 15 | |
| α-helix | 1514-1519 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 19 | 1 | 4 |
| β-strand | 28-30 | 3 | 9 |
| β-strand | 35-37 | 3 | 9 |
| β-strand | 38-44 | 7 | 4 |
| β-strand | 50-56 | 7 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein PaFPC1 | A | protein | 1596 | Periplaneta americana | D0E0C2 (AlphaFold model) |
| Mu-diguetoxin-Dc1a | B | protein | 57 | Diguetia canities | P49126 (AlphaFold model) |
>6A95_1 Sodium channel protein PaFPC1 (chains A) MASWSHPQFEKGGGARGGSGGGSWSHPQFEKGFDYKDDDDKGTMADNSPLIREERQRLFR PYTRAMLTAPSAQPAKENGKTEENKDNSRDKGRGANKDRDGSAHPDQALEQGSRLPARMR NIFPAELASTPLEDFDPFYKNKKTFVVVTKAGDIFRFSGEKSLWMLDPFTPIRRVAISTM VQPIFSYFIMITILIHCIFMIMPATQTTYILELVFLSIYTIEVVVKVLARGFILHPFAYL RDPWNWLDFLVTLIGYITLVVDLGHLYALRAFRVLRSWRTVTIVPGWRTIVDALSLSITS LKDLVLLLLFSLFVFAVLGLQIYMGVLTQKCVKHFPADGSWGNFTDERWFNYTSNSSHWY IPDDWIEYPLCGNSSGAGMCPPGYTCLQGYGGNPNYGYTSFDTFGWAFLSVFRLVTLDYW EDLYQLALRSAGPWHILFFIIVVFYGTFCFLNFILAVVVMSYTHMVKRADEEKAAERELK KEKKAASVANNTANGQEQTTIEMNGDEAVVIDNNDQAARQQSDPETPAPSVTQRLTDFLC VWDCCVPWQKLQGAIGAVVLSPFFELFIAVIIVLNITFMALDHHDMNIEFERILRTGNYI FTSIYIVEAVLKIIALSPKFYFKDSWNVFDFIIVVFAILELGLEGVQGLSVFRSFRLLRV FRLAKFWPTLNNFMSVMTKSYGAFVNVMYVMFLLLFIFAIIGMQLFGMNYIDNMERFPDG DLPRWNFTDFLHSFMIVFRALCGEWIESMWDCMLVGDWSCIPFFVAVFFVGNLVILNLLI ALLLNNYGSFCTSPTSDEEDSKDEDALAQIVRIFKRFKPNLNAVKLSPMKPDSEDIVESQ EIQGNNIADAEDVLAGEFPPDCCCNAFYKCFPSRPARDSSVQRMWSNIRRVCFLLAKNKY FQKFVTAVLVITSVLLALEDIYLPQRPVLVNITLYVDYVLTAFFVIEMIIMLFAVGFKKY FTSKWYWLDFIVVVAYLLNFVLMCAGIEALQTLRLLRVFRLFRPLSKVNGMQVVTSTLVE AVPHIFNVILVGIFFWLVFAIMGVQLFAGKFYKCVDENSTVLSHEITMDRNDCLHENYTW ENSPMNFDHVGNAYLSLLQVATFKGWLQIMNDAIDSREVHKQPIRETNIYMYLYFIFFIV FGSFFILKLFVCILIDIFRQQRRKAEGLSATDSRTQLIYRRAVMRTMSAKPVKRIPKPTC HPQSLMYDISVNRKFEYTMMILIILNVAVMAIDHYGQSMEFSEVLDYLNLIFIIIFFVEC VIKVSGLRHHYFKDPWNIIDFLYVVLAIAGLMLSDVIEKYFISPTLLRILRILRVGRLLR YFQSARGMRLLLLALRKALRTLFNVSFLLFVIMFVYAVFGMEFFMHIRDAGAIDDVYNFK TFGQSIILLFQLATSAGWDGVYFAIANEEDCRAPDHELGYPGNCGSRALGIAYLVSYLII TCLVVINMYAAVILDYVLEVYEDSKEGLTDDDYDMFFEVWQQFDPEATQYIRYDQLSELL EALQPPLQVQKPNKYKILSMNIPICKDDHIFYKDVLEALVKDVFSRRGSPVEAGDVQAPN VDEAEYKPVSSTLQRQREEYCVRLIQNAWRKHKQQN
>6A95_2 Mu-diguetoxin-Dc1a (chains B) SAKDGDVEGPAGCKKYDVECDSGECCQKQYLWYKWRPLDCRCLKSGFFSSKCVCRDV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 9SR | (1R,5R,6R,7R,9S,11S,12S,13S,14S)-3-amino-14-(hydroxymethyl)-8,10-dioxa-2,4-diaz… | C11 H17 N3 O8 | 1 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
Water and common crystallization additives (NA) are not listed.
Structural basis for the modulation of voltage-gated sodium channels by animal toxins. Shen, H., Li, Z., Jiang, Y. et al. Science (2018) 362. DOI 10.1126/science.aau2596 · 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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