Complex of voltage-gated sodium channel NavPaS from American cockroach Periplaneta americana and Dc1a. Determined by electron microscopy at 2.8 Å resolution. Released 8 Aug 2018.
Explore 6A90 in 3D Show helices and sheets RCSB PDB PDBe
6A90 contains 85 α-helices and 23 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 | 53-55 | 3 | |
| α-helix | 56-60 | 5 | |
| α-helix | 98-109 | 12 | |
| α-helix | 130-137 | 8 | |
| α-helix | 142-158 | 17 | |
| α-helix | 160-161 | 2 | |
| α-helix | 163-182 | 20 | |
| α-helix | 196-198 | 3 | |
| α-helix | 204-216 | 13 | |
| α-helix | 226-235 | 10 | |
| α-helix | 238-240 | 3 | |
| α-helix | 244-257 | 14 | |
| α-helix | 259-279 | 21 | |
| α-helix | 283-285 | 3 | |
| β-strand | 287-290 | 4 | 1 |
| α-helix | 291-293 | 3 | |
| α-helix | 305-311 | 7 | |
| α-helix | 313-315 | 3 | |
| β-strand | 316 | 1 | 1 |
| α-helix | 325-327 | 3 | |
| α-helix | 337-338 | 2 | |
| β-strand | 341-344 | 4 | 1 |
| α-helix | 361-373 | 13 | |
| α-helix | 377-385 | 9 | |
| α-helix | 390-392 | 3 | |
| α-helix | 393-399 | 7 | |
| α-helix | 400-407 | 8 | |
| α-helix | 408-434 | 27 | |
| α-helix | 503-516 | 14 | |
| α-helix | 521-537 | 17 | |
| β-strand | 543-544 | 2 | 2 |
| α-helix | 545-570 | 26 | |
| α-helix | 575-578 | 4 | |
| α-helix | 582-599 | 18 | |
| α-helix | 609-619 | 11 | |
| α-helix | 620-623 | 4 | |
| α-helix | 625-636 | 12 | |
| α-helix | 639-662 | 24 | |
| α-helix | 666-669 | 4 | |
| α-helix | 671-673 | 3 | |
| α-helix | 687-698 | 12 | |
| α-helix | 703-711 | 9 | |
| α-helix | 717-725 | 9 | |
| α-helix | 726-732 | 7 | |
| α-helix | 733-735 | 3 | |
| α-helix | 737-743 | 7 | |
| α-helix | 836-853 | 18 | |
| α-helix | 856-871 | 16 | |
| α-helix | 873-875 | 3 | |
| α-helix | 884-917 | 34 | |
| α-helix | 921-941 | 21 | |
| α-helix | 944-947 | 4 | |
| α-helix | 948-951 | 4 | |
| α-helix | 952-958 | 7 | |
| α-helix | 959-962 | 4 | |
| α-helix | 968-977 | 10 | |
| α-helix | 979-1004 | 26 | |
| β-strand | 1009-1012 | 4 | 3 |
| β-strand | 1018 | 1 | 3 |
| α-helix | 1019-1020 | 2 | |
| β-strand | 1026 | 1 | 4 |
| α-helix | 1027-1032 | 6 | |
| β-strand | 1036-1039 | 4 | 3 |
| α-helix | 1047-1058 | 12 | |
| α-helix | 1063-1072 | 10 | |
| β-strand | 1078 | 1 | 4 |
| α-helix | 1086-1088 | 3 | |
| α-helix | 1089-1095 | 7 | |
| α-helix | 1096-1100 | 5 | |
| α-helix | 1105-1122 | 18 | |
| α-helix | 1133-1141 | 9 | |
| α-helix | 1148-1155 | 8 | |
| α-helix | 1162-1165 | 4 | |
| α-helix | 1170-1185 | 16 | |
| α-helix | 1186-1189 | 4 | |
| α-helix | 1198-1223 | 26 | |
| α-helix | 1228-1230 | 3 | |
| α-helix | 1232-1248 | 17 | |
| α-helix | 1261-1269 | 9 | |
| α-helix | 1270-1277 | 8 | |
| α-helix | 1283-1321 | 39 | |
| β-strand | 1327 | 1 | 5 |
| β-strand | 1330 | 1 | 5 |
| α-helix | 1339-1348 | 10 | |
| α-helix | 1349-1351 | 3 | |
| α-helix | 1355-1362 | 8 | |
| β-strand | 1372 | 1 | 6 |
| β-strand | 1377 | 1 | 6 |
| α-helix | 1384-1394 | 11 | |
| α-helix | 1395-1402 | 8 | |
| α-helix | 1404-1422 | 19 | |
| α-helix | 1427-1437 | 11 | |
| β-strand | 1447-1449 | 3 | 7 |
| α-helix | 1451-1459 | 9 | |
| α-helix | 1461 | 1 | |
| α-helix | 1471-1477 | 7 | |
| β-strand | 1486-1488 | 3 | 7 |
| α-helix | 1489-1504 | 16 | |
| α-helix | 1509-1519 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-8 | 2 | 8 |
| β-strand | 14 | 1 | 9 |
| β-strand | 19 | 1 | 2 |
| β-strand | 25 | 1 | 9 |
| β-strand | 28-30 | 3 | 8 |
| β-strand | 35-36 | 2 | 8 |
| α-helix | 37 | 1 | |
| β-strand | 38-44 | 7 | 2 |
| β-strand | 50-56 | 7 | 2 |
| 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) |
>6A90_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
>6A90_2 Mu-diguetoxin-Dc1a (chains B) SAKDGDVEGPAGCKKYDVECDSGECCQKQYLWYKWRPLDCRCLKSGFFSSKCVCRDV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 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:
MolViewer shows 6A90 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.