Cryo-EM structure of a human sodium pump W931R mutant in ouabain-bound E2P state. Determined by electron microscopy at 2.86 Å resolution. Released 27 May 2026.
Explore 9WAK in 3D Show helices and sheets RCSB PDB PDBe
9WAK contains 62 α-helices and 51 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 | 43-45 | 3 | |
| α-helix | 50-51 | 2 | |
| α-helix | 52-56 | 5 | |
| α-helix | 65-75 | 11 | |
| α-helix | 80-84 | 5 | |
| α-helix | 88-96 | 9 | |
| α-helix | 100-119 | 20 | |
| α-helix | 128-159 | 32 | |
| α-helix | 164-167 | 4 | |
| β-strand | 168 | 1 | 1 |
| β-strand | 171-173 | 3 | 2 |
| β-strand | 176-178 | 3 | 2 |
| β-strand | 181 | 1 | 1 |
| α-helix | 182-184 | 3 | |
| β-strand | 190-194 | 5 | 2 |
| β-strand | 198 | 1 | 2 |
| β-strand | 202-214 | 13 | 2 |
| β-strand | 225-227 | 3 | 2 |
| β-strand | 242-243 | 2 | 2 |
| α-helix | 244 | 1 | |
| β-strand | 248-260 | 13 | 2 |
| α-helix | 262-264 | 3 | |
| α-helix | 266-276 | 11 | |
| α-helix | 283-312 | 30 | |
| α-helix | 317-330 | 14 | |
| α-helix | 334-352 | 19 | |
| β-strand | 356-358 | 3 | 3 |
| α-helix | 362-364 | 3 | |
| α-helix | 366-369 | 4 | |
| β-strand | 372-375 | 4 | 3 |
| α-helix | 377-381 | 5 | |
| β-strand | 382 | 1 | 4 |
| β-strand | 387-393 | 7 | 5 |
| β-strand | 396-399 | 4 | 5 |
| α-helix | 416-427 | 12 | |
| β-strand | 432-433 | 2 | 6 |
| β-strand | 447-448 | 2 | 6 |
| α-helix | 451-463 | 13 | |
| α-helix | 467-473 | 7 | |
| β-strand | 476 | 1 | 7 |
| β-strand | 493 | 1 | 7 |
| β-strand | 507-509 | 3 | 5 |
| α-helix | 511-516 | 6 | |
| β-strand | 518-523 | 6 | 5 |
| β-strand | 526-529 | 4 | 5 |
| α-helix | 534-542 | 9 | |
| β-strand | 551-557 | 7 | 5 |
| β-strand | 583-592 | 10 | 5 |
| α-helix | 594 | 1 | |
| β-strand | 595 | 1 | 4 |
| α-helix | 596 | 1 | |
| α-helix | 599-607 | 9 | |
| α-helix | 611 | 1 | |
| β-strand | 612-616 | 5 | 3 |
| α-helix | 621-631 | 11 | |
| α-helix | 643-647 | 5 | |
| α-helix | 657-659 | 3 | |
| β-strand | 662-666 | 5 | 3 |
| α-helix | 667-671 | 5 | |
| α-helix | 678-684 | 7 | |
| β-strand | 687-691 | 5 | 3 |
| α-helix | 695-707 | 13 | |
| β-strand | 712-716 | 5 | 3 |
| α-helix | 719-721 | 3 | |
| α-helix | 722-727 | 6 | |
| β-strand | 730-734 | 5 | 3 |
| α-helix | 740-745 | 6 | |
| β-strand | 748-750 | 3 | 3 |
| α-helix | 756-781 | 26 | |
| α-helix | 783-796 | 14 | |
| α-helix | 804-808 | 5 | |
| α-helix | 809-814 | 6 | |
| α-helix | 817-821 | 5 | |
| α-helix | 822-824 | 3 | |
| α-helix | 835-837 | 3 | |
| α-helix | 847-851 | 5 | |
| α-helix | 852-856 | 5 | |
| α-helix | 857-876 | 20 | |
| α-helix | 880-882 | 3 | |
| α-helix | 887-890 | 4 | |
| β-strand | 898-899 | 2 | 8 |
| β-strand | 905-906 | 2 | 8 |
| α-helix | 908-938 | 31 | |
| α-helix | 974-976 | 3 | |
| α-helix | 982-984 | 3 | |
| α-helix | 992-1011 | 20 | |
| α-helix | 1016-1021 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 24 | 1 | 9 |
| β-strand | 27 | 1 | 9 |
| α-helix | 29-58 | 30 | |
| β-strand | 76 | 1 | 10 |
| β-strand | 77-80 | 4 | 11 |
| β-strand | 87-90 | 4 | 12 |
| α-helix | 99-108 | 10 | |
| β-strand | 123-124 | 2 | 13 |
| α-helix | 146-147 | 2 | |
| β-strand | 148-149 | 2 | 13 |
| α-helix | 153-159 | 7 | |
| β-strand | 175-180 | 6 | 11 |
| α-helix | 181-182 | 2 | |
| β-strand | 184 | 1 | 14 |
| β-strand | 208-210 | 3 | 15 |
| β-strand | 211-215 | 5 | 12 |
| α-helix | 218-224 | 7 | |
| β-strand | 227-230 | 4 | 11 |
| β-strand | 237-239 | 3 | 15 |
| α-helix | 240-242 | 3 | |
| β-strand | 245 | 1 | 14 |
| β-strand | 259-263 | 5 | 11 |
| α-helix | 266-267 | 2 | |
| β-strand | 271-278 | 8 | 12 |
| β-strand | 292 | 1 | 10 |
| β-strand | 294-301 | 8 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium/potassium-transporting ATPase subunit alpha-1 | A | protein | 985 | Homo sapiens | P05023 (AlphaFold model) |
| Sodium/potassium-transporting ATPase subunit beta-1 | B | protein | 303 | Homo sapiens | P05026 (AlphaFold model) |
>9WAK_1 Sodium/potassium-transporting ATPase subunit alpha-1 (chains A) VSMDDHKLSLDELHRKYGTDLSRGLTSARAAEILARDGPNALTPPPTTPEWIKFCRQLFG GFSMLLWIGAILCFLAYSIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIM ESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSL TGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLE GGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVIFLIGIIVANVPEGLLA TVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIH EADTTENQSGVSFDKTSATWLALSRIAGLCNRAVFQANQENLPILKRAVAGDASESALLK CIELCCGSVKEMRERYAKIVEIPFNSTNKYQLSIHKNPNTSEPQHLLVMKGAPERILDRC SSILLHGKEQPLDEELKDAFQNAYLELGGLGERVLGFCHLFLPDEQFPEGFQFDTDDVNF PIDNLCFVGLISMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGN ETVEDIAARLNIPVSQVNPRDAKACVVHGSDLKDMTSEQLDDILKYHTEIVFARTSPQQK LIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASI VTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLIFIIANIPLPLGTVTILCIDLGTDMVP AISLAYEQAESDIMKRQPRNPKTDKLVNERLISMAYGQIGMIQALGGFFTYFVILAENGF LPIHLLGLRVDWDDRWINDVEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQRADLVICK TRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMGVALRMYPLKPTWWFCAFPYSLLI FVYDEVRKLIIRRRPGGWVEKETYY
>9WAK_2 Sodium/potassium-transporting ATPase subunit beta-1 (chains B) MARGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYGCLAGIFIGTIQVMLLT ISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLNIVRFLEKYKDSAQRDD MIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLNDETYGYKEGKPCIIIKL NRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKVGNVEYFGLGNSPGFPL QYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIGYSEKDRFQGRFDVKIE VKS
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
| OBN | Ouabain | C29 H44 O12 | 1 |
| CLR | Cholesterol | C27 H46 O | 12 |
| BEF | Beryllium trifluoride ion | Be F3 | 1 |
Water and common crystallization additives (NA) are not listed.
Passive aberrant currents are induced by all Na pump variants causing hypomagnesemia. Artigas, P., Abe, K. To be published.
Other PDB entries of the same protein (UniProt P05023 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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