Human alpha3 Na+,K+-ATPase in the Na+-bound E1-ATP state obtained under turnover conditions. Determined by electron microscopy at 3.27 Å resolution. Released 12 Aug 2026.
Explore 9ROF in 3D Show helices and sheets RCSB PDB PDBe
9ROF contains 67 α-helices and 47 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 | 79-87 | 9 | |
| α-helix | 92-107 | 16 | |
| α-helix | 117-153 | 37 | |
| β-strand | 158-163 | 6 | 1 |
| β-strand | 166-171 | 6 | 1 |
| β-strand | 180-183 | 4 | 1 |
| β-strand | 187-188 | 2 | 2 |
| β-strand | 193-199 | 7 | 1 |
| β-strand | 202-204 | 3 | 2 |
| α-helix | 206-209 | 4 | |
| β-strand | 214-216 | 3 | 2 |
| β-strand | 232-233 | 2 | 1 |
| β-strand | 238-239 | 2 | 2 |
| β-strand | 243-248 | 6 | 1 |
| α-helix | 252-254 | 3 | |
| α-helix | 273-302 | 30 | |
| α-helix | 307-320 | 14 | |
| α-helix | 325-343 | 19 | |
| β-strand | 346-348 | 3 | 3 |
| α-helix | 353-358 | 6 | |
| β-strand | 362-365 | 4 | 3 |
| β-strand | 372 | 1 | 4 |
| β-strand | 377-383 | 7 | 5 |
| β-strand | 386-389 | 4 | 5 |
| β-strand | 390 | 1 | 6 |
| β-strand | 399 | 1 | 6 |
| α-helix | 406-418 | 13 | |
| β-strand | 422-423 | 2 | 7 |
| α-helix | 424 | 1 | |
| α-helix | 432-434 | 3 | |
| β-strand | 437-438 | 2 | 7 |
| α-helix | 441-452 | 12 | |
| α-helix | 458-461 | 4 | |
| β-strand | 466 | 1 | 5 |
| β-strand | 481-483 | 3 | 5 |
| β-strand | 494-499 | 6 | 5 |
| α-helix | 501-504 | 4 | |
| α-helix | 505-507 | 3 | |
| β-strand | 510-513 | 4 | 5 |
| β-strand | 516-519 | 4 | 5 |
| α-helix | 522-538 | 17 | |
| β-strand | 540-549 | 10 | 5 |
| α-helix | 560-562 | 3 | |
| β-strand | 574-582 | 9 | 5 |
| α-helix | 584 | 1 | |
| β-strand | 585 | 1 | 4 |
| α-helix | 586 | 1 | |
| α-helix | 589-598 | 10 | |
| β-strand | 602-605 | 4 | 3 |
| 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 | 3 |
| α-helix | 657-662 | 6 | |
| α-helix | 665-674 | 10 | |
| β-strand | 677-681 | 5 | 3 |
| α-helix | 685-697 | 13 | |
| β-strand | 702-706 | 5 | 3 |
| α-helix | 712-717 | 6 | |
| β-strand | 720-724 | 5 | 3 |
| α-helix | 730-735 | 6 | |
| β-strand | 738-740 | 3 | 3 |
| α-helix | 745-771 | 27 | |
| α-helix | 778-785 | 8 | |
| α-helix | 794-801 | 8 | |
| α-helix | 802-806 | 5 | |
| α-helix | 807-811 | 5 | |
| α-helix | 812-814 | 3 | |
| α-helix | 815-818 | 4 | |
| α-helix | 821-823 | 3 | |
| α-helix | 825-827 | 3 | |
| α-helix | 837-840 | 4 | |
| α-helix | 841-847 | 7 | |
| α-helix | 848-865 | 18 | |
| α-helix | 870-872 | 3 | |
| 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 | 975-979 | 5 | |
| α-helix | 982-1001 | 20 | |
| α-helix | 1006-1011 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 29-58 | 30 | |
| α-helix | 70-72 | 3 | |
| β-strand | 77-79 | 3 | 9 |
| β-strand | 87-89 | 3 | 10 |
| α-helix | 95-98 | 4 | |
| α-helix | 99-109 | 11 | |
| α-helix | 110-112 | 3 | |
| α-helix | 114-117 | 4 | |
| α-helix | 153-156 | 4 | |
| β-strand | 175-180 | 6 | 9 |
| α-helix | 181-182 | 2 | |
| β-strand | 184 | 1 | 11 |
| β-strand | 208-210 | 3 | 12 |
| β-strand | 211-215 | 5 | 10 |
| α-helix | 218-223 | 6 | |
| β-strand | 227-230 | 4 | 9 |
| α-helix | 232-234 | 3 | |
| β-strand | 237-239 | 3 | 12 |
| α-helix | 243 | 1 | |
| β-strand | 245 | 1 | 11 |
| α-helix | 256-257 | 2 | |
| β-strand | 258-263 | 6 | 9 |
| β-strand | 271-278 | 8 | 10 |
| β-strand | 294-300 | 7 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-55 | 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) |
>9ROF_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
>9ROF_2 Sodium/potassium-transporting ATPase subunit beta-1 (chains B) MARSHHHHHHHHHHPRRSRGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYG CLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLN IVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLND ETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKV GNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIG YSEKDRFQGRFDVKIEVKS
>9ROF_3 Phospholemman (chains C) GTKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEE EGTFRSSIRRLSTRRR
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
| ATP | Adenosine-5'-triphosphate | C10 H16 N5 O13 P3 | 1 |
| CLR | Cholesterol | C27 H46 O | 3 |
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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