Human alpha3 Na+,K+-ATPase in the Na+-bound E1-ATP state. Determined by electron microscopy at 3.27 Å resolution. Released 12 Aug 2026.
Explore 9RO9 in 3D Show helices and sheets RCSB PDB PDBe
9RO9 contains 62 α-helices and 49 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 | |
| α-helix | 55-65 | 11 | |
| α-helix | 71-73 | 3 | |
| α-helix | 78-87 | 10 | |
| α-helix | 92-107 | 16 | |
| α-helix | 117 | 1 | |
| α-helix | 118-122 | 5 | |
| α-helix | 123-153 | 31 | |
| β-strand | 158-163 | 6 | 1 |
| β-strand | 166-171 | 6 | 1 |
| β-strand | 180-184 | 5 | 1 |
| β-strand | 187-189 | 3 | 1 |
| β-strand | 192-205 | 14 | 1 |
| β-strand | 211-216 | 6 | 1 |
| β-strand | 232-233 | 2 | 1 |
| β-strand | 237-250 | 14 | 1 |
| α-helix | 252-254 | 3 | |
| α-helix | 273-302 | 30 | |
| α-helix | 307-320 | 14 | |
| α-helix | 326-343 | 18 | |
| β-strand | 346-347 | 2 | 2 |
| α-helix | 351-353 | 3 | |
| α-helix | 354-358 | 5 | |
| β-strand | 362-365 | 4 | 2 |
| β-strand | 377-383 | 7 | 3 |
| β-strand | 386-389 | 4 | 3 |
| α-helix | 406-418 | 13 | |
| β-strand | 422-423 | 2 | 4 |
| α-helix | 424 | 1 | |
| α-helix | 427-429 | 3 | |
| β-strand | 437-438 | 2 | 4 |
| α-helix | 441-453 | 13 | |
| α-helix | 457-463 | 7 | |
| β-strand | 466-468 | 3 | 3 |
| β-strand | 481-483 | 3 | 3 |
| β-strand | 494-496 | 3 | 3 |
| β-strand | 499 | 1 | 3 |
| α-helix | 501-506 | 6 | |
| β-strand | 510-513 | 4 | 3 |
| β-strand | 516-519 | 4 | 3 |
| α-helix | 522-537 | 16 | |
| β-strand | 541-549 | 9 | 3 |
| β-strand | 574-582 | 9 | 3 |
| α-helix | 584-586 | 3 | |
| α-helix | 589-598 | 10 | |
| β-strand | 602-605 | 4 | 2 |
| α-helix | 611-621 | 11 | |
| β-strand | 630 | 1 | 2 |
| α-helix | 631-638 | 8 | |
| α-helix | 642-644 | 3 | |
| α-helix | 647-649 | 3 | |
| β-strand | 652-655 | 4 | 2 |
| α-helix | 657-661 | 5 | |
| α-helix | 665-674 | 10 | |
| β-strand | 677-680 | 4 | 2 |
| α-helix | 685-696 | 12 | |
| β-strand | 702-706 | 5 | 2 |
| α-helix | 709-711 | 3 | |
| α-helix | 712-717 | 6 | |
| β-strand | 720-724 | 5 | 2 |
| α-helix | 730-735 | 6 | |
| β-strand | 738-740 | 3 | 2 |
| α-helix | 745-771 | 27 | |
| α-helix | 774-785 | 12 | |
| α-helix | 794-804 | 11 | |
| α-helix | 807-812 | 6 | |
| α-helix | 815-817 | 3 | |
| α-helix | 825-827 | 3 | |
| α-helix | 837-840 | 4 | |
| α-helix | 841-848 | 8 | |
| α-helix | 849-866 | 18 | |
| α-helix | 870-872 | 3 | |
| α-helix | 877-881 | 5 | |
| β-strand | 888-889 | 2 | 5 |
| β-strand | 895-896 | 2 | 5 |
| α-helix | 898-927 | 30 | |
| α-helix | 934-937 | 4 | |
| α-helix | 942-960 | 19 | |
| α-helix | 964-967 | 4 | |
| α-helix | 975-979 | 5 | |
| α-helix | 982-1001 | 20 | |
| α-helix | 1006-1011 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 29-60 | 32 | |
| α-helix | 70-72 | 3 | |
| β-strand | 76 | 1 | 6 |
| β-strand | 77-79 | 3 | 7 |
| β-strand | 87-89 | 3 | 8 |
| α-helix | 99-108 | 10 | |
| α-helix | 116-118 | 3 | |
| β-strand | 123-124 | 2 | 9 |
| α-helix | 125 | 1 | |
| α-helix | 133-134 | 2 | |
| β-strand | 148-149 | 2 | 9 |
| α-helix | 153-156 | 4 | |
| β-strand | 177-180 | 4 | 7 |
| β-strand | 184 | 1 | 10 |
| β-strand | 208-210 | 3 | 11 |
| β-strand | 211-215 | 5 | 8 |
| α-helix | 218-224 | 7 | |
| β-strand | 227 | 1 | 12 |
| β-strand | 230 | 1 | 7 |
| β-strand | 237-239 | 3 | 11 |
| α-helix | 240-242 | 3 | |
| α-helix | 243-244 | 2 | |
| β-strand | 245 | 1 | 10 |
| β-strand | 258-260 | 3 | 7 |
| β-strand | 263 | 1 | 12 |
| β-strand | 271-278 | 8 | 8 |
| β-strand | 292 | 1 | 6 |
| β-strand | 294-300 | 7 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-56 | 24 |
| 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) |
>9RO9_1 Sodium/potassium-transporting ATPase subunit alpha-3 (chains A) MGDKKDDKDSPKKNKGKERRDLDDLKKEVAMTEHKMSVEEVCRKYNTDCVQGLTHSKAQE ILARDGPNALTPPPTTPEWVKFCRQLFGGFSILLWIGAILCFLAYGIQAGTEDDPSGDNL YLGIVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIREGEKMQVNAEEVVVGDL VEIKGGDRVPADLRIISAHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNITFFSTNCV EGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAIEIEHFIQLITGVAVFLGVSFFILS LILGYTWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGST STICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGTSFDKSSHTWVALSHIAGLCNR AVFKGGQDNIPVLKRDVAGDASESALLKCIELSSGSVKLMRERNKKVAEIPFNSTNKYQL SIHETEDPNDNRYLLVMKGAPERILDRCSTILLQGKEQPLDEEMKEAFQNAYLELGGLGE RVLGFCHYYLPEEQFPKGFAFDCDDVNFTTDNLCFVGLMSMIDPPRAAVPDAVGKCRSAG IKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVIHGTDL KDFTSEQIDEILQNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADI GVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPF LLFIMANIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLVNERLI SMAYGQIGMIQALGGFFSYFVILAENGFLPGNLVGIRLNWDDRTVNDLEDSYGQQWTYEQ RKVVEFTCHTAFFVSIVVVQWADLIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSY CPGMDVALRMYPLKPSWWFCAFPYSFLIFVYDEIRKLILRRNPGGWVEKETYY
>9RO9_2 Sodium/potassium-transporting ATPase subunit beta-1 (chains B) MARSHHHHHHHHHHPRRSRGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYG CLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLN IVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLND ETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKV GNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIG YSEKDRFQGRFDVKIEVKS
>9RO9_3 Phospholemman (chains C) GTKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEE EGTFRSSIRRLSTRRR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| CLR | Cholesterol | C27 H46 O | 3 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
| MG | Magnesium ion | Mg | 1 |
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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