9ROH: PDB entry 9ROH

Human alpha3 Na+,K+-ATPase in the Na+-occluded E2P state obtained under turnover conditions. Determined by electron microscopy at 2.92 Å resolution. Released 12 Aug 2026.

Method: Electron microscopy
Resolution: 2.92 Å
Organism: Homo sapiens
Chains: 3
Atoms: 10,301
Mol. weight: 159.8 kDa
Ligands: CLR, NAG
Released: 12 Aug 2026

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

Secondary structure: helices and β-sheets

9ROH contains 62 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.

Chain A: 49 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	39-44	6
α-helix	55-65	11
α-helix	71-73	3
α-helix	82-86	5
α-helix	91-111	21
α-helix	118-148	31
β-strand	158-163	6	1
β-strand	166-171	6	1
β-strand	180-184	5	1
β-strand	187-188	2	2
β-strand	192-199	8	1
β-strand	203	1	2
α-helix	214-216	3
β-strand	232-233	2	1
β-strand	238-239	2	2
β-strand	243-250	8	1
α-helix	256-266	11
α-helix	273-303	31
α-helix	307-321	15
α-helix	326-343	18
β-strand	348	1	3
α-helix	351-358	8
β-strand	362-363	2	3
β-strand	372	1	4
β-strand	377-383	7	5
β-strand	386-388	3	5
α-helix	406-418	13
β-strand	422	1	6
β-strand	438	1	6
α-helix	441-453	13
α-helix	458-461	4
β-strand	465-470	6	5
β-strand	478-484	7	5
β-strand	493-499	7	5
α-helix	501-506	6
β-strand	508-513	6	5
β-strand	516-518	3	5
α-helix	522-537	16
β-strand	541-548	8	5
β-strand	573-582	10	5
α-helix	584	1
β-strand	585	1	4
α-helix	586	1
α-helix	589-598	10
β-strand	602-603	2	3
β-strand	605-606	2	7
α-helix	611-621	11
α-helix	631-638	8
α-helix	642-644	3
α-helix	647-649	3
β-strand	654-656	3	7
α-helix	659-661	3
α-helix	665-674	10
β-strand	679-681	3	7
α-helix	685-697	13
β-strand	702-706	5	3
α-helix	709-711	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	746-770	25
α-helix	773-785	13
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	870-873	4
α-helix	877-881	5
β-strand	888-889	2	8
β-strand	895-896	2	8
α-helix	898-927	30
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	1006-1010	5

Chain B: 12 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	29-60	32
α-helix	75-76	2
β-strand	77-79	3	9
β-strand	87-90	4	10
α-helix	99-109	11
α-helix	110-112	3
α-helix	114-117	4
β-strand	123-124	2	11
α-helix	132-134	3
α-helix	146-147	2
β-strand	148-149	2	11
α-helix	153-156	4
β-strand	175-180	6	9
α-helix	181-182	2
β-strand	184	1	12
α-helix	205-207	3
β-strand	208-210	3	13
β-strand	211-216	6	10
β-strand	226-230	5	9
β-strand	237-239	3	13
α-helix	240-242	3
β-strand	245	1	12
α-helix	247-250	4
β-strand	258-264	7	9
β-strand	272-278	7	10
β-strand	294-301	8	10

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	33-56	24

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

>9ROH_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

>9ROH_2 Sodium/potassium-transporting ATPase subunit beta-1 (chains B)
MARSHHHHHHHHHHPRRSRGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYG
CLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLN
IVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLND
ETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKV
GNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIG
YSEKDRFQGRFDVKIEVKS

Sequence of entity 3 (C), FASTA

>9ROH_3 Phospholemman (chains C)
GTKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEE
EGTFRSSIRRLSTRRR

Ligands and cofactors

ID	Name	Formula	Copies
CLR	Cholesterol	C27 H46 O	3
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	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…
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
9ROD 3.12 Å, Human alpha3 Na+,K+-ATPase in the Na+-occluded E2P 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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