9ROG: PDB entry 9ROG

Human alpha3 Na+,K+-ATPase in the Na+-occluded E1P-ADP state obtained under turnover conditions. Determined by electron microscopy at 2.8 Å resolution. Released 12 Aug 2026.

Method: Electron microscopy
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 3
Atoms: 10,156
Mol. weight: 160.23 kDa
Ligands: MG, NAG, PO3, ADP
Released: 12 Aug 2026

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

Secondary structure: helices and β-sheets

9ROG contains 64 α-helices and 51 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: 52 helices, 33 β-strands

Element	Residues	Length	Sheet
α-helix	38-44	7
α-helix	55-65	11
α-helix	70-77	8
α-helix	78-86	9
α-helix	91-108	18
β-strand	109	1	1
β-strand	112	1	1
α-helix	118-151	34
β-strand	158-163	6	2
β-strand	166-171	6	2
α-helix	172-174	3
β-strand	178-183	6	2
β-strand	187-188	2	2
β-strand	192-204	13	2
β-strand	215-216	2	2
β-strand	232-233	2	2
β-strand	238-250	13	2
α-helix	252-254	3
α-helix	256-259	4
α-helix	273-303	31
α-helix	307-320	14
α-helix	326-343	18
β-strand	347-348	2	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
α-helix	406-418	13
β-strand	422-423	2	6
β-strand	437-438	2	6
α-helix	441-453	13
α-helix	457-463	7
β-strand	466-470	5	5
β-strand	478-483	6	5
β-strand	494-499	6	5
α-helix	501-507	7
β-strand	508-513	6	5
β-strand	516-519	4	5
α-helix	522-537	16
β-strand	540-548	9	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	602-606	5	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	665-673	9
β-strand	677-681	5	3
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	747-770	24
α-helix	773-785	13
α-helix	794-804	11
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	841-848	8
α-helix	849-866	18
α-helix	870-872	3
α-helix	877-881	5
β-strand	888-889	2	7
β-strand	895-896	2	7
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	1008-1011	4

Chain B: 11 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	29-60	32
β-strand	76	1	8
β-strand	77-79	3	9
β-strand	87-90	4	10
α-helix	95-98	4
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	153-159	7
β-strand	175-180	6	9
β-strand	184	1	12
α-helix	190-192	3
β-strand	208-210	3	13
β-strand	211-215	5	10
β-strand	228-230	3	9
β-strand	231	1	14
β-strand	233	1	14
β-strand	237-239	3	13
α-helix	240-242	3
β-strand	245	1	12
α-helix	247-250	4
β-strand	258-262	5	9
β-strand	272-278	7	10
β-strand	292	1	8
β-strand	294-301	8	10

Chain C: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	33-55	23

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

>9ROG_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

>9ROG_2 Sodium/potassium-transporting ATPase subunit beta-1 (chains B)
MARSHHHHHHHHHHPRRSRGKAKEEGSWKKFIWNSEKKEFLGRTGGSWFKILLFYVIFYG
CLAGIFIGTIQVMLLTISEFKPTYQDRVAPPGLTQIPQIQKTEISFRPNDPKSYEAYVLN
IVRFLEKYKDSAQRDDMIFEDCGDVPSEPKERGDFNHERGERKVCRFKLEWLGNCSGLND
ETYGYKEGKPCIIIKLNRVLGFKPKPPKNESLETYPVMKYNPNVLPVQCTGKRDEDKDKV
GNVEYFGLGNSPGFPLQYYPYYGKLLQPKYLQPLLAVQFTNLTMDTEIRIECKAYGENIG
YSEKDRFQGRFDVKIEVKS

Sequence of entity 3 (C), FASTA

>9ROG_3 Phospholemman (chains C)
GTKAESPKEHDPFTYDYQSLQIGGLVIAGILFILGILIVLSRRCRCKFNQQQRTGEPDEE
EGTFRSSIRRLSTRRR

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	3
PO3	Phosphite ion	O3 P	1
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	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:

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
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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