9W2S: ATP synthase F complex subunit 8

Cryo-EM structure of FoF1-ATPase monomer state 3 on the bovine heart submitochondrial particles (FoF1-2). Determined by electron microscopy at 4.0 Å resolution. Released 1 Apr 2026.

Method: Electron microscopy
Resolution: 4.0 Å
Organism: Bos taurus
Chains: 29
Atoms: 39,116
Mol. weight: 588.98 kDa
Released: 1 Apr 2026

Explore 9W2S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9W2S contains 285 α-helices and 183 β-strands across 29 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 8: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	6-8	3
α-helix	11-18	8
α-helix	19-23	5
α-helix	25-29	5

Chain a: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	4-9	6
α-helix	20-22	3
α-helix	27-30	4
α-helix	41-58	18
α-helix	63-85	23
α-helix	94-96	3
α-helix	98-103	6
α-helix	106-115	10
α-helix	122-126	5
α-helix	139-180	42
α-helix	181-183	3
α-helix	186-224	39

Chain A: 26 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
β-strand	25-26	2	9
β-strand	28-35	8	1
β-strand	38-43	6	1
α-helix	47-48	2
β-strand	52-55	4	1
β-strand	60-66	7	1
β-strand	71-75	5	1
α-helix	79-81	3
β-strand	87-90	4	1
β-strand	96-99	4	10
α-helix	101-103	3
β-strand	107-108	2	11
β-strand	125-128	4	10
α-helix	131-134	4
β-strand	139	1	12
β-strand	145	1	13
α-helix	151-155	5
β-strand	160	1	13
β-strand	164	1	11
β-strand	166-169	4	14
α-helix	175-185	11
α-helix	187-191	5
β-strand	200-206	7	11
α-helix	210-223	14
α-helix	226-228	3
β-strand	229-234	6	11
α-helix	240-259	20
β-strand	263-267	5	11
α-helix	271-284	14
α-helix	287-289	3
α-helix	291-293	3
α-helix	298-306	9
β-strand	311	1	11
β-strand	312	1	12
α-helix	314-316	3
β-strand	320-324	5	11
β-strand	326-328	3	14
α-helix	337-343	7
β-strand	348-351	4	14
β-strand	352	1	15
α-helix	354-358	5
β-strand	365	1	15
β-strand	371-372	2	14
α-helix	381-399	19
α-helix	401-405	5
α-helix	412-427	16
α-helix	438-450	13
α-helix	452-455	4
α-helix	461-475	15
α-helix	477-485	9
α-helix	491-507	17

Chain b: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	9-11	3
β-strand	12-13	2	47
β-strand	17-18	2	47
α-helix	20-29	10
α-helix	32-37	6
α-helix	43-47	5
α-helix	55-115	61
α-helix	116-120	5
α-helix	123-184	62
α-helix	190-208	19

Chain B: 26 helices, 31 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	19-22	4
β-strand	28-35	8	1
β-strand	38-43	6	1
α-helix	47-48	2
β-strand	51-55	5	1
β-strand	60-66	7	1
β-strand	71-75	5	1
α-helix	79-81	3
β-strand	87-94	8	1
β-strand	96-99	4	16
α-helix	101-103	3
β-strand	107-108	2	17
β-strand	114	1	17
β-strand	125-128	4	16
α-helix	131-134	4
β-strand	139	1	18
β-strand	145-146	2	19
α-helix	151-156	6
β-strand	159-160	2	19
β-strand	164	1	17
β-strand	166-169	4	20
α-helix	177-190	14
β-strand	200-204	5	17
β-strand	208	1	21
α-helix	210-221	12
α-helix	225-228	4
β-strand	229-232	4	17
β-strand	235	1	21
α-helix	240-259	20
β-strand	263-268	6	17
α-helix	271-284	14
α-helix	287-289	3
α-helix	291-293	3
α-helix	298-306	9
β-strand	311	1	17
β-strand	312	1	18
α-helix	314-316	3
β-strand	320-325	6	17
β-strand	326-328	3	20
α-helix	337-343	7
β-strand	348	1	22
β-strand	349-351	3	20
β-strand	352	1	23
α-helix	354-358	5
β-strand	365	1	23
β-strand	367	1	24
β-strand	370	1	24
β-strand	372	1	22
α-helix	375-378	4
α-helix	381-401	21
α-helix	413-428	16
α-helix	435-437	3
α-helix	438-449	12
α-helix	461-475	15
α-helix	477-486	10
α-helix	491-508	18

Chain C: 24 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	28-35	8	1
β-strand	38-43	6	1
α-helix	47-48	2
β-strand	52-55	4	1
β-strand	60-66	7	1
β-strand	71-75	5	1
β-strand	87-90	4	1
β-strand	96-99	4	2
β-strand	107-108	2	3
β-strand	114	1	3
β-strand	125-128	4	2
α-helix	131-134	4
β-strand	139	1	4
β-strand	145-146	2	5
α-helix	151-156	6
β-strand	159-160	2	5
β-strand	164	1	3
β-strand	166-169	4	6
α-helix	172-174	3
α-helix	176-185	10
α-helix	187-190	4
β-strand	201-208	8	3
α-helix	210-223	14
α-helix	226-228	3
β-strand	229-235	7	3
α-helix	240-259	20
β-strand	263-268	6	3
α-helix	271-284	14
α-helix	287-289	3
α-helix	291-293	3
α-helix	298-306	9
β-strand	311	1	3
β-strand	312	1	4
α-helix	314-316	3
β-strand	320-324	5	3
β-strand	326-328	3	6
α-helix	337-343	7
β-strand	348	1	7
β-strand	349-351	3	6
β-strand	352	1	8
α-helix	354-357	4
β-strand	365	1	8
β-strand	372	1	7
α-helix	375-377	3
α-helix	381-399	19
α-helix	401-404	4
α-helix	412-427	16
α-helix	438-449	12
α-helix	461-475	15
α-helix	477-486	10
α-helix	491-506	16

Chain d: 12 helices, 0 β-strands

Element	Residues	Length
α-helix	12-14	3
α-helix	15-18	4
α-helix	21-26	6
α-helix	27-41	15
α-helix	53-59	7
α-helix	65-75	11
α-helix	85-90	6
α-helix	91-100	10
α-helix	104-122	19
α-helix	124-126	3
α-helix	132-138	7
α-helix	140-142	3

Chain D: 25 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	1
β-strand	20-25	6	1
α-helix	29-31	3
β-strand	35-38	4	1
β-strand	46-54	9	1
β-strand	57-62	6	1
β-strand	75-77	3	1
β-strand	83-86	4	30
α-helix	88-90	3
β-strand	94-95	2	31
β-strand	101	1	31
β-strand	112-115	4	30
α-helix	120-122	3
α-helix	123-125	3
β-strand	132-133	2	32
α-helix	138-143	6
β-strand	146-147	2	32
β-strand	151-156	6	31
α-helix	163-169	7
α-helix	170-174	5
β-strand	180-186	7	31
α-helix	190-203	14
β-strand	215-220	6	31
α-helix	226-229	4
α-helix	232-247	16
β-strand	251-255	5	31
α-helix	259-269	11
α-helix	270-272	3
β-strand	277	1	33
β-strand	281	1	33
α-helix	285-294	10
β-strand	304-311	8	31
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	31
β-strand	335	1	34
α-helix	337-341	5
β-strand	348	1	34
β-strand	354-355	2	31
α-helix	360-363	4
α-helix	365-391	27
α-helix	393-395	3
α-helix	398-413	16
α-helix	422-425	4
α-helix	434-446	13
α-helix	454-457	4
α-helix	463-476	14

21 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ATP synthase F(0) complex subunit 8	8	protein	66	Bos taurus	P03929 (AlphaFold model)
ATP synthase F(1) complex subunit alpha, mitochondrial	A, B, C	protein	510	Bos taurus	P19483 (AlphaFold model)
ATP synthase F(1) complex catalytic subunit beta, mitochondrial	D, E, F	protein	482	Bos taurus	P00829 (AlphaFold model)
ATP synthase F(1) complex subunit gamma, mitochondrial	G	protein	273	Bos taurus	P05631 (AlphaFold model)
ATP synthase F(1) complex subunit delta, mitochondrial	H	protein	146	Bos taurus	P05630
ATP synthase F(1) complex subunit epsilon, mitochondrial	I	protein	50	Bos taurus	P05632
ATPase inhibitor, mitochondrial	J	protein	60	Bos taurus	P01096
ATP synthase F(0) complex subunit C1, mitochondrial	K, L, M, N, O, P, Q, R	protein	75	Bos taurus	P32876
ATP synthase peripheral stalk subunit OSCP, mitochondrial	S	protein	190	Bos taurus	P13621
ATP synthase F(0) complex subunit a	a	protein	226	Bos taurus	P00847
ATP synthase peripheral stalk subunit b, mitochondrial	b	protein	214	Bos taurus	P13619
ATP synthase peripheral stalk subunit d, mitochondrial	d	protein	160	Bos taurus	P13620

6 more molecules are not listed.

Sequence of entity 1 (8), FASTA

>9W2S_1 ATP synthase F(0) complex subunit 8 (chains 8)
MPQLDTSTWLTMILSMFLTLFIIFQLKVSKHNFYHNPELTPTKMLKQNTPWETKWTKIYL
PLLLPL

Sequence of entity 2 (A, B, C), FASTA

>9W2S_2 ATP synthase F(1) complex subunit alpha, mitochondrial (chains A, B, C)
QKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
SKIRTDGKISEESDAKLKEIVTNFLAGFEA

Sequence of entity 3 (D, E, F), FASTA

>9W2S_3 ATP synthase F(1) complex catalytic subunit beta, mitochondrial (chains D, E, F)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS

Sequence of entity 4 (G), FASTA

>9W2S_4 ATP synthase F(1) complex subunit gamma, mitochondrial (chains G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAALD

Sequence of entity 5 (H), FASTA

>9W2S_5 ATP synthase F(1) complex subunit delta, mitochondrial (chains H)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE

Sequence of entity 6 (I), FASTA

>9W2S_6 ATP synthase F(1) complex subunit epsilon, mitochondrial (chains I)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

Sequence of entity 7 (J), FASTA

>9W2S_7 ATPase inhibitor, mitochondrial (chains J)
GSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEI

Sequence of entity 8 (K, L, M, N, O, P, Q, R), FASTA

>9W2S_8 ATP synthase F(0) complex subunit C1, mitochondrial (chains K, L, M, N, O, P, Q, R)
DIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAM
GLFCLMVAFLILFAM

Sequence of entity 9 (S), FASTA

>9W2S_9 ATP synthase peripheral stalk subunit OSCP, mitochondrial (chains S)
FAKLVRPPVQIYGIEGRYATALYSAASKQNKLEQVEKELLRVGQILKEPKMAASLLNPYV
KRSVKVKSLSDMTAKEKFSPLTSNLINLLAENGRLTNTPAVISAFSTMMSVHRGEVPCTV
TTASALDEATLTELKTVLKSFLSKGQVLKLEVKIDPSIMGGMIVRIGEKYVDMSAKTKIQ
KLSRAMREIL

Sequence of entity 10 (a), FASTA

>9W2S_10 ATP synthase F(0) complex subunit a (chains a)
MNENLFTSFITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSI
HNSKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNK
TKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLA
LMSISTTTALITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT

Sequence of entity 11 (b), FASTA

>9W2S_11 ATP synthase peripheral stalk subunit b, mitochondrial (chains b)
PVPPLPEHGGKVRFGLIPEEFFQFLYPKTGVTGPYVLGTGLILYLLSKEIYVITPETFSA
ISTIGFLVYIVKKYGASVGEFADKLNEQKIAQLEEVKQASIKQIQDAIDMEKSQQALVQK
RHYLFDVQRNNIAMALEVTYRERLHRVYREVKNRLDYHISVQNMMRQKEQEHMINWVEKR
VVQSISAQQEKETIAKCIADLKLLSKKAQAQPVM

Sequence of entity 12 (d), FASTA

>9W2S_12 ATP synthase peripheral stalk subunit d, mitochondrial (chains d)
AGRKLALKTIDWVAFGEIIPRNQKAVANSLKSWNETLTSRLATLPEKPPAIDWAYYKANV
AKAGLVDDFEKKFNALKVPIPEDKYTAQVDAEEKEDVKSCAEFLTQSKTRIQEYEKELEK
MRNIIPFDQMTIEDLNEVFPETKLDKKKYPYWPHRPIETL

Primary citation

Structures of respiratory supercomplexes and ATP synthase oligomers in mammalian mitochondrial inner membrane. Nakano, A., Masuya, T., Akisada, S. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-70578-x · PubMed

Other PDB entries of the same protein (UniProt P03929 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ZQM 3.29 Å, bovine ATP synthase monomer state 2 (combined)
9W2R 3.4 Å, Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial…
6ZIT 3.49 Å, bovine ATP synthase Stator domain, state 2
6ZBB 3.61 Å, bovine ATP synthase Fo domain
6ZPO 4.0 Å, bovine ATP synthase monomer state 1 (combined)
6ZQN 4.0 Å, bovine ATP synthase monomer state 3 (combined)
9W2T 4.1 Å, Cryo-EM structure of Fo domain of FoF1-ATPase monomer state on the bovine heart…
6ZIQ 4.33 Å, bovine ATP synthase stator domain, state 1
9VPB 5.0 Å, Cryo-EM structure of the IF1 bound bovine F-ATP synthase planar dimer
6ZIU 6.02 Å, bovine ATP synthase stator domain, state 3
9VPC 7.2 Å, Cryo-EM structure of the IF1 bound bovine ATP synthase tetramer
7AJF 8.45 Å, bovine ATP synthase dimer state2:state2

Browse structure collections

About this viewer

MolViewer shows 9W2S directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.