Human SCNN1D-SCNN1B-SCNN1G ENaC trimer. Determined by electron microscopy at 3.38 Å resolution. Released 27 Nov 2024.
Explore 9BLR in 3D Show helices and sheets RCSB PDB PDBe
9BLR contains 48 α-helices and 70 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 | 130-134 | 5 | 1 |
| α-helix | 142-144 | 3 | |
| α-helix | 145-162 | 18 | |
| β-strand | 193-195 | 3 | 2 |
| β-strand | 205-211 | 7 | 2 |
| β-strand | 214-222 | 9 | 2 |
| α-helix | 225-241 | 17 | |
| β-strand | 260-265 | 6 | 3 |
| β-strand | 268-270 | 3 | 3 |
| α-helix | 272-274 | 3 | |
| β-strand | 276-280 | 5 | 1 |
| β-strand | 284-288 | 5 | 1 |
| α-helix | 294-295 | 2 | |
| α-helix | 300-302 | 3 | |
| β-strand | 304-309 | 6 | 3 |
| β-strand | 323 | 1 | 4 |
| β-strand | 325-330 | 6 | 1 |
| β-strand | 343-345 | 3 | 1 |
| β-strand | 349-361 | 13 | 3 |
| β-strand | 371 | 1 | 5 |
| β-strand | 372 | 1 | 6 |
| β-strand | 375 | 1 | 6 |
| α-helix | 389-405 | 17 | |
| β-strand | 408 | 1 | 7 |
| β-strand | 420 | 1 | 7 |
| α-helix | 429-441 | 13 | |
| α-helix | 447-450 | 4 | |
| α-helix | 452-453 | 2 | |
| β-strand | 454 | 1 | 5 |
| β-strand | 456-468 | 13 | 3 |
| α-helix | 475-485 | 11 | |
| β-strand | 498-505 | 8 | 3 |
| β-strand | 512-513 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 79-86 | 8 | 4 |
| β-strand | 90-91 | 2 | 8 |
| α-helix | 92-93 | 2 | |
| β-strand | 94-99 | 6 | 9 |
| α-helix | 105-108 | 4 | |
| α-helix | 113-127 | 15 | |
| α-helix | 129-131 | 3 | |
| α-helix | 142-145 | 4 | |
| β-strand | 150-154 | 5 | 10 |
| β-strand | 162-165 | 4 | 10 |
| α-helix | 182-184 | 3 | |
| β-strand | 189-197 | 9 | 10 |
| β-strand | 202-208 | 7 | 10 |
| α-helix | 211-227 | 17 | |
| α-helix | 232-235 | 4 | |
| α-helix | 242-245 | 4 | |
| β-strand | 246-251 | 6 | 4 |
| β-strand | 254-256 | 3 | 4 |
| α-helix | 258-260 | 3 | |
| β-strand | 262-266 | 5 | 9 |
| β-strand | 270-275 | 6 | 9 |
| α-helix | 282-284 | 3 | |
| β-strand | 285-286 | 2 | 8 |
| α-helix | 291-293 | 3 | |
| β-strand | 295-300 | 6 | 4 |
| α-helix | 303-305 | 3 | |
| β-strand | 314 | 1 | 11 |
| β-strand | 316-321 | 6 | 9 |
| α-helix | 329-332 | 4 | |
| β-strand | 334-336 | 3 | 9 |
| β-strand | 340-352 | 13 | 4 |
| β-strand | 362 | 1 | 12 |
| α-helix | 373-377 | 5 | |
| α-helix | 379-381 | 3 | |
| α-helix | 383-399 | 17 | |
| β-strand | 402 | 1 | 13 |
| β-strand | 414 | 1 | 13 |
| α-helix | 423-432 | 10 | |
| α-helix | 434-441 | 8 | |
| α-helix | 444-446 | 3 | |
| β-strand | 447 | 1 | 12 |
| β-strand | 449-450 | 2 | 4 |
| β-strand | 453 | 1 | 4 |
| β-strand | 456-461 | 6 | 4 |
| α-helix | 468-477 | 10 | |
| β-strand | 492-511 | 20 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 82-89 | 8 | 11 |
| β-strand | 92-93 | 2 | 14 |
| β-strand | 96-101 | 6 | 15 |
| α-helix | 107-128 | 22 | |
| α-helix | 153-157 | 5 | |
| β-strand | 160-162 | 3 | 16 |
| β-strand | 202-206 | 5 | 16 |
| β-strand | 215-219 | 5 | 16 |
| α-helix | 222-238 | 17 | |
| α-helix | 243-248 | 6 | |
| α-helix | 253-256 | 4 | |
| β-strand | 257-262 | 6 | 11 |
| β-strand | 265-267 | 3 | 11 |
| α-helix | 269-271 | 3 | |
| β-strand | 272-277 | 6 | 15 |
| β-strand | 281-286 | 6 | 15 |
| α-helix | 293-295 | 3 | |
| β-strand | 296-297 | 2 | 14 |
| α-helix | 302-304 | 3 | |
| β-strand | 306-311 | 6 | 11 |
| α-helix | 314-316 | 3 | |
| β-strand | 325 | 1 | 3 |
| β-strand | 327-332 | 6 | 15 |
| α-helix | 340-343 | 4 | |
| β-strand | 345-347 | 3 | 15 |
| β-strand | 351-363 | 13 | 11 |
| β-strand | 373 | 1 | 17 |
| α-helix | 391-405 | 15 | |
| β-strand | 410 | 1 | 18 |
| β-strand | 422 | 1 | 18 |
| α-helix | 431-442 | 12 | |
| α-helix | 449-452 | 4 | |
| β-strand | 456 | 1 | 17 |
| β-strand | 458-462 | 5 | 11 |
| β-strand | 465-470 | 6 | 11 |
| α-helix | 477-487 | 11 | |
| α-helix | 495-497 | 3 | |
| α-helix | 498-500 | 3 | |
| β-strand | 501-519 | 19 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Isoform 1 of Amiloride-sensitive sodium channel subunit delta | A | protein | 638 | Homo sapiens | P51172 (AlphaFold model) |
| Amiloride-sensitive sodium channel subunit beta | B | protein | 640 | Homo sapiens | P51168 (AlphaFold model) |
| Amiloride-sensitive sodium channel subunit gamma | C | protein | 649 | Homo sapiens | P51170 (AlphaFold model) |
>9BLR_1 Isoform 1 of Amiloride-sensitive sodium channel subunit delta (chains A) MAEHRSMDGRMEAATRGGSHLQAAAQTPPRPGPPSAPPPPPKEGHQEGLVELPASFRELL TFFATNATIHGAIRLVCSRGNRLKTTSWGLLSLGALVALCWQLGLLFERHWHRPVLMAVS VHSERKLLPLVTLCDGNPRRPSPVLRHLELLDEFARENIDSLYNVNLSKGRAALSATVPR HEPPFHLDREIRLQRLSHSGSRVRVGFRLCNSTGGDCFYRGYTSGVAAVQDWYHFHYVDI LALLPAAWEDSHGSQDGHFVLSCSYDGLDCQARQFRTFHHPTYGSCYTVDGVWTAQRPGI THGVGLVLRVEQQPHLPLLSTLAGIRVMVHGRNHTPFLGHHSFSVRPGTEATISIREDEV HRLGSPYGHCTAGGEGVEVELLHNTSYTRQACLVSCFQQLMVETCSCGYYLHPLPAGAEY CSSARHPAWGHCFYRLYQDLETHRLPCTSRCPRPCRESAFKLSTGTSRWPSAKSAGWTLA TLGEQGLPHQSHRQRSSLAKINIVYQELNYRSVEEAPVYSVPQLLSAMGSLCSLWFGASV LSLLELLELLLDASALTLVLGGRRLRRAWFSWPRASPASGASSIKPEASQMPPPAGGTSD DPEPSGPHLPRVMLPGVLAGVSAEESWAGPQPLETLDT
>9BLR_2 Amiloride-sensitive sodium channel subunit beta (chains B) MHVKKYLLKGLHRLQKGPGYTYKELLVWYADNTNTHGPKRIICEGPKKKAMWFLLTLLFA ALVCWQWGIFIRTYLSWEVSVSLSVGFKTMDFPAVTICNASPFKYSKIKHLLKDLDELME AVLERILAPELSHANATRNLNFSIWNHTPLVLIDERNPHHPMVLDLFGDNHNGLTSSSAS EKICNAHGCKMAMRLCSLNRTQCTFRNFTSATQALTEWYILQATNIFAQVPQQELVEMSY PGEQMILACLFGAEPCNYRNFTSIFYPHYGNCYIFNWGMTEKALPSANPGTEFGLKLILD IGQEDYVPFLASTAGVRLMLHEQRSYPFIRDEGIYAMSGTETSIGVLVDKLQRMGEPYSP CTVNGSEVPVQNFYSDYNTTYSIQACLRSCFQDHMIRNCNCGHYLYPLPRGEKYCNNRDF PDWAHCYSDLQMSVAQRETCIGMCKESCNDTQYKMTISMADWPSEASEDWIFHVLSQERD QSTNITLSRKGIVKLNIYFQEFNYRTIEESAANNIVWLLSNLGGQFGFWMGGSVLCLIEF GEIIIDFVWITIIKLVALAKSLRQRRAQASYAGPPPTVAELVEAHTNFGFQPDTAPRSPN TGPYPSEQALPIPGTPPPNYDSLRLQPLDVIESDSEGDAI
>9BLR_3 Amiloride-sensitive sodium channel subunit gamma (chains C) MAPGEKIKAKIKKNLPVTGPQAPTIKELMRWYALNTNTHGARRIVVSRGRLRRLLWIGFT LTAVALILWQCALLVFSFYTVSVSIKVHFRKLDFPAVTICNINPYKYSTVRHLLADLEQE TREALKSLYGFPESRKRAEAESWNSVSEGKQPRFSHRIPLLIFDQDEKGKARDFFTGRKR KVGGSIIHKASNVMHIESKQVVGFQLCSNDTSDCATYTFSSGINAIQEWYKLHYMNIMAQ VPLEKKINMSYSAEELLVTCFFDGVSCDARNFTLFHHPMHGNCYTFNNRENETILSTSMG GSEYGLQVILYINEEEYNPFLVSSTGAKVIIHRQDEYPFVEDVGTEIETAMVTSIGMHLT ESFKLSEPYSQCTEDGSDVPIRNIYNAAYSLQICLHSCFQTKMVEKCGCAQYSQPLPPAA NYCNYQQHPNWMYCYYQLHRAFVQEELGCQSVCKEACSFKEWTLTTSLAQWPSVVSEKWL LPVLTWDQGRQVNKKLNKTDLAKLLIFYKDLNQRSIMESPANSIEMLLSNFGGQLGLWMS CSVVCVIEIIEVFFIDFFSIIARRQWQKAKEWWAWKQAPPCPEAPRSPQGQDNPALDIDD DLPTFNSALHLPPALGTQVPGTPPPKYNTLRLERAFSNQLTDTQMLDEL
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 6 |
Structural insights into subunit-dependent functional regulation in epithelial sodium channels. Houser, A., Baconguis, I. Structure (2025) 33:349-362.e4. DOI 10.1016/j.str.2024.11.013 · PubMed
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