9ROD: PDB entry 9ROD

Human alpha3 Na+,K+-ATPase in the Na+-occluded E2P state. Determined by electron microscopy at 3.12 Å resolution. Released 12 Aug 2026.

Method: Electron microscopy
Resolution: 3.12 Å
Organism: Homo sapiens
Chains: 3
Atoms: 10,330
Mol. weight: 160.23 kDa
Ligands: NAG, CLR
Released: 12 Aug 2026

Explore 9ROD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9ROD contains 65 α-helices and 44 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.

Chain A: 51 helices, 30 β-strands

Element	Residues	Length	Sheet
α-helix	38-44	7
α-helix	55-65	11
α-helix	71-73	3
α-helix	81-86	6
α-helix	91-111	21
α-helix	118-148	31
β-strand	158-163	6	1
β-strand	166-171	6	1
β-strand	180-183	4	1
β-strand	187-188	2	1
β-strand	192-203	12	1
α-helix	214	1
β-strand	215-216	2	1
α-helix	217	1
β-strand	232-233	2	1
β-strand	238-250	13	1
α-helix	256-264	9
α-helix	273-302	30
α-helix	307-320	14
α-helix	326-343	18
β-strand	346-348	3	2
α-helix	351-358	8
β-strand	362-365	4	2
α-helix	367-371	5
β-strand	377-383	7	3
β-strand	386-389	4	3
α-helix	406-418	13
β-strand	422	1	4
α-helix	432-434	3
β-strand	438	1	4
α-helix	441-454	14
α-helix	458-462	5
β-strand	464-470	7	3
β-strand	478-485	8	3
β-strand	493-499	7	3
α-helix	501-507	7
β-strand	508-513	6	3
β-strand	516-518	3	3
α-helix	522-537	16
β-strand	541-550	10	3
β-strand	573-582	10	3
α-helix	584-586	3
α-helix	588-598	11
β-strand	602-606	5	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	652-656	5	2
α-helix	665-674	10
β-strand	677-681	5	2
α-helix	685-697	13
β-strand	702-706	5	2
α-helix	709-711	3
α-helix	712-717	6
β-strand	720-724	5	2
α-helix	730-734	5
β-strand	738-740	3	2
α-helix	746-771	26
α-helix	773-785	13
α-helix	794-804	11
α-helix	807-813	7
α-helix	815-818	4
α-helix	821-823	3
α-helix	825-828	4
α-helix	837-840	4
α-helix	841-848	8
α-helix	849-866	18
α-helix	870-873	4
α-helix	877-881	5
β-strand	888-889	2	5
β-strand	895-896	2	5
α-helix	898-926	29
α-helix	934-937	4
α-helix	942-960	19
α-helix	964-967	4
α-helix	972-974	3
α-helix	975-980	6
α-helix	982-1001	20
α-helix	1006-1011	6

Chain B: 13 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	29-60	32
α-helix	75-76	2
β-strand	77-79	3	6
β-strand	87-90	4	7
α-helix	95-97	3
α-helix	99-110	12
α-helix	114-117	4
α-helix	132-134	3
α-helix	146-147	2
α-helix	153-156	4
β-strand	175-180	6	6
α-helix	181-182	2
β-strand	184	1	8
α-helix	188-191	4
α-helix	205-207	3
β-strand	208-210	3	9
β-strand	211-212	2	10
β-strand	216	1	7
β-strand	228-230	3	6
β-strand	237-239	3	9
α-helix	240-242	3
β-strand	245	1	8
α-helix	256-258	3
β-strand	259-262	4	6
β-strand	272-275	4	7
β-strand	277-278	2	10
β-strand	296-301	6	7

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	33-57	25

Molecules and chains

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)

Sequence of entity 1 (A), FASTA

>9ROD_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

Sequence of entity 2 (B), FASTA

>9ROD_2 Sodium/potassium-transporting ATPase subunit beta-1 (chains B)
MARSHHHHHHHHHHPRRSRGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYG
CLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLN
IVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLND
ETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKV
GNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIG
YSEKDRFQGRFDVKIEVKS

Sequence of entity 3 (C), FASTA

>9ROD_3 Phospholemman (chains C)
GTKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEE
EGTFRSSIRRLSTRRR

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	1
CLR	Cholesterol	C27 H46 O	3

Water and common crystallization additives (NA) are not listed.

Primary citation

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:

9ROG 2.8 Å, Human alpha3 Na+,K+-ATPase in the Na+-occluded E1P-ADP state obtained under turnover…
9ROH 2.92 Å, Human alpha3 Na+,K+-ATPase in the Na+-occluded E2P state obtained under turnover…
9ROE 2.94 Å, Human alpha3 Na+,K+-ATPase in the outward open E2P state
9ROI 2.94 Å, Human alpha3 Na+,K+-ATPase in the K+-occluded E2P state obtained under turnover conditions
9ROA 3.08 Å, Human alpha3 Na+,K+-ATPase in the Na+-occluded E1P-ADP state
9RO9 3.27 Å, Human alpha3 Na+,K+-ATPase in the Na+-bound E1-ATP state
9ROF 3.27 Å, Human alpha3 Na+,K+-ATPase in the Na+-bound E1-ATP state obtained under turnover…
8D3V 3.4 Å, Human alpha3 Na+/K+-ATPase in its cytoplasmic side-open state
8D3W 3.5 Å, Human alpha3 Na+/K+-ATPase in its AMPPCP-bound cytoplasmic side-open state
9ROL 3.54 Å, Human alpha3 Q140L Na+,K+-ATPase in the Na+-occluded E2P state
9ROJ 3.58 Å, Human alpha3 Q140L Na+,K+-ATPase in the Na+-bound E1 state
9ROM 3.6 Å, Human alpha3 Q140L Na+,K+-ATPase in the outward open E2P state

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