Human alpha3 Q140L Na+,K+-ATPase in the Na+-bound E1 state. Determined by electron microscopy at 3.58 Å resolution. Released 12 Aug 2026.
Explore 9ROJ in 3D Show helices and sheets RCSB PDB PDBe
9ROJ contains 61 α-helices and 50 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 | 38-44 | 7 | |
| β-strand | 48 | 1 | 1 |
| β-strand | 52 | 1 | 1 |
| α-helix | 55-65 | 11 | |
| α-helix | 79-87 | 9 | |
| α-helix | 92-104 | 13 | |
| α-helix | 118-151 | 34 | |
| β-strand | 158-163 | 6 | 2 |
| β-strand | 166-171 | 6 | 2 |
| α-helix | 172-174 | 3 | |
| β-strand | 180-184 | 5 | 2 |
| β-strand | 187-189 | 3 | 2 |
| β-strand | 192-205 | 14 | 2 |
| β-strand | 213-216 | 4 | 2 |
| β-strand | 232-233 | 2 | 2 |
| α-helix | 234 | 1 | |
| β-strand | 237-250 | 14 | 2 |
| α-helix | 273-302 | 30 | |
| α-helix | 307-321 | 15 | |
| α-helix | 326-343 | 18 | |
| β-strand | 346-347 | 2 | 3 |
| α-helix | 351-357 | 7 | |
| β-strand | 362-365 | 4 | 4 |
| β-strand | 372 | 1 | 5 |
| β-strand | 377-383 | 7 | 6 |
| β-strand | 386-389 | 4 | 6 |
| α-helix | 406-418 | 13 | |
| β-strand | 422 | 1 | 7 |
| β-strand | 438 | 1 | 7 |
| α-helix | 441-453 | 13 | |
| α-helix | 457-463 | 7 | |
| α-helix | 465 | 1 | |
| β-strand | 466 | 1 | 6 |
| β-strand | 479-483 | 5 | 6 |
| β-strand | 494-499 | 6 | 6 |
| α-helix | 501-505 | 5 | |
| β-strand | 508-513 | 6 | 6 |
| β-strand | 516-519 | 4 | 6 |
| α-helix | 522-537 | 16 | |
| β-strand | 541-548 | 8 | 6 |
| β-strand | 573-582 | 10 | 6 |
| α-helix | 584 | 1 | |
| β-strand | 585 | 1 | 5 |
| α-helix | 586 | 1 | |
| α-helix | 589-598 | 10 | |
| β-strand | 602-605 | 4 | 4 |
| α-helix | 611-621 | 11 | |
| α-helix | 631-638 | 8 | |
| α-helix | 642-644 | 3 | |
| α-helix | 647-649 | 3 | |
| β-strand | 652-656 | 5 | 4 |
| α-helix | 657-662 | 6 | |
| α-helix | 665-674 | 10 | |
| β-strand | 677-681 | 5 | 4 |
| α-helix | 685-697 | 13 | |
| β-strand | 702-704 | 3 | 4 |
| α-helix | 712-717 | 6 | |
| β-strand | 720-721 | 2 | 4 |
| β-strand | 722-724 | 3 | 3 |
| α-helix | 730-735 | 6 | |
| β-strand | 738-740 | 3 | 3 |
| α-helix | 745-771 | 27 | |
| α-helix | 778-785 | 8 | |
| α-helix | 794-804 | 11 | |
| α-helix | 807-811 | 5 | |
| α-helix | 812-814 | 3 | |
| α-helix | 815-817 | 3 | |
| α-helix | 825-828 | 4 | |
| α-helix | 837-840 | 4 | |
| α-helix | 841-847 | 7 | |
| α-helix | 848-866 | 19 | |
| α-helix | 870-873 | 4 | |
| α-helix | 877-881 | 5 | |
| β-strand | 888-889 | 2 | 8 |
| β-strand | 895-896 | 2 | 8 |
| α-helix | 898-926 | 29 | |
| α-helix | 934-937 | 4 | |
| α-helix | 942-960 | 19 | |
| α-helix | 964-967 | 4 | |
| α-helix | 975-978 | 4 | |
| α-helix | 982-1001 | 20 | |
| α-helix | 1006-1011 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 29-60 | 32 | |
| β-strand | 76 | 1 | 9 |
| β-strand | 77-79 | 3 | 10 |
| β-strand | 87-89 | 3 | 11 |
| α-helix | 99-108 | 10 | |
| α-helix | 116-118 | 3 | |
| β-strand | 123-124 | 2 | 12 |
| α-helix | 133-134 | 2 | |
| α-helix | 146-147 | 2 | |
| β-strand | 148-149 | 2 | 12 |
| α-helix | 153-155 | 3 | |
| β-strand | 175-180 | 6 | 10 |
| α-helix | 181-182 | 2 | |
| β-strand | 184 | 1 | 13 |
| α-helix | 205-207 | 3 | |
| β-strand | 208-210 | 3 | 14 |
| β-strand | 212-215 | 4 | 11 |
| α-helix | 218-224 | 7 | |
| β-strand | 227-230 | 4 | 10 |
| α-helix | 232-234 | 3 | |
| β-strand | 237-239 | 3 | 14 |
| α-helix | 243 | 1 | |
| β-strand | 245 | 1 | 13 |
| α-helix | 247-250 | 4 | |
| β-strand | 258-263 | 6 | 10 |
| β-strand | 271-277 | 7 | 11 |
| β-strand | 292 | 1 | 9 |
| β-strand | 294-300 | 7 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-56 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium/potassium-transporting ATPase subunit alpha-3 | A | protein | 1013 | Homo sapiens | P13637 (AlphaFold model) |
| Sodium/potassium-transporting ATPase subunit beta-1 | B | protein | 319 | Homo sapiens | P05026 (AlphaFold model) |
| Phospholemman | C | protein | 76 | Homo sapiens | O00168 (AlphaFold model) |
>9ROJ_1 Sodium/potassium-transporting ATPase subunit alpha-3 (chains A) MGDKKDDKDSPKKNKGKERRDLDDLKKEVAMTEHKMSVEEVCRKYNTDCVQGLTHSKAQE ILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAGTEDDPSGDNL YLGIVLAAVVIITGCFSYYLEAKSSKIMESFKNMVPQQALVIREGEKMQVNAEEVVVGDL VEIKGGDRVPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNITFFSTNCV EGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAIEIEHFIQLITGVAVFLGVSFFILS LILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGST STICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGTSFDKSSHTWVALSHIAGLCNR AVFKGGQDNIPVLKRDVAGDASESALLKCIELSSGSVKLMRERNKKVAEIPFNSTNKYQL SIHETEDPNDNRYLLVMKGAPERILDRCSTILLQGKEQPLDEEMKEAFQNAYLELGGLGE RVLGFCHYYLPEEQFPKGFAFDCDDVNFTTDNLCFVGLMSMIDPPRAAVPDAVGKCRSAG IKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVIHGTDL KDFTSEQIDEILQNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADI GVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPF LLFIMANIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLVNERLI SMAYGQIGMIQALGGFFSYFVILAENGFLPGNLVGIRLNWDDRTVNDLEDSYGQQWTYEQ RKVVEFTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSY CPGMDVALRMYPLKPSWWFCAFPYSFLIFVYDEIRKLILRRNPGGWVEKETYY
>9ROJ_2 Sodium/potassium-transporting ATPase subunit beta-1 (chains B) MARSHHHHHHHHHHPRRSRGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYG CLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLN IVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLND ETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKV GNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIG YSEKDRFQGRFDVKIEVKS
>9ROJ_3 Phospholemman (chains C) GTKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEE EGTFRSSIRRLSTRRR
Water and common crystallization additives (NA) are not listed.
Active conformations of neuronal Na + , K + -ATPase isoforms and a disease-causing mutant. Christensen, M.E., Habeck, M., Katz, A. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-75997-4 · PubMed
Other PDB entries of the same protein (UniProt P13637 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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