7AJD: Bovine ATP synthase dimer state1:state3

bovine ATP synthase dimer state1:state3. Determined by electron microscopy at 9.0 Å resolution. Released 3 Feb 2021.

Method: Electron microscopy
Resolution: 9.0 Å
Organism: Bos taurus
Chains: 58
Atoms: 51,424
Mol. weight: 1191.11 kDa
Ligands: LHG, CDL
Released: 3 Feb 2021

Explore 7AJD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7AJD contains 511 α-helices and 382 β-strands across 58 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	2-4	3
α-helix	6-16	11
α-helix	17-23	7
α-helix	24-29	6

Chain a: 13 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	6-9	4
α-helix	11-12	2
α-helix	20-25	6
α-helix	26-30	5
β-strand	36	1	96
α-helix	41-58	18
α-helix	63-66	4
α-helix	69-86	18
α-helix	98-119	22
α-helix	122-126	5
α-helix	135-137	3
α-helix	138-180	43
α-helix	181-183	3
α-helix	186-224	39

Chain A: 22 helices, 32 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
β-strand	28-35	8	1
β-strand	38-43	6	1
α-helix	47	1
β-strand	48	1	2
β-strand	51-55	5	1
β-strand	60-66	7	1
β-strand	71-75	5	1
β-strand	87-94	8	1
β-strand	96-99	4	3
α-helix	101-103	3
β-strand	107-109	3	4
β-strand	114	1	4
β-strand	125-128	4	3
β-strand	139	1	5
β-strand	145	1	6
α-helix	151-156	6
β-strand	160	1	6
β-strand	164	1	4
β-strand	167-169	3	7
α-helix	175-184	10
α-helix	187-191	5
β-strand	200-206	7	4
α-helix	210-222	13
β-strand	229-234	6	4
α-helix	240-259	20
β-strand	263-269	7	4
α-helix	271-284	14
α-helix	287-288	2
β-strand	289	1	8
α-helix	291-293	3
β-strand	295	1	8
α-helix	299-306	8
β-strand	311	1	4
β-strand	312	1	5
β-strand	320-323	4	4
β-strand	326-328	3	7
α-helix	337-345	9
β-strand	348-349	2	9
β-strand	350-351	2	7
β-strand	352	1	10
α-helix	355-358	4
β-strand	365	1	10
β-strand	367	1	11
β-strand	370	1	11
β-strand	371-372	2	9
α-helix	375-378	4
α-helix	381-398	18
α-helix	402-405	4
α-helix	412-428	17
α-helix	438-449	12
α-helix	458-475	18
α-helix	477-486	10
α-helix	491-506	16

Chain A8: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	2-4	3
α-helix	6-8	3
α-helix	9-17	9
α-helix	18-23	6
α-helix	24-29	6
α-helix	34-37	4

Chain Aa: 13 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	7-9	3
α-helix	11-12	2
α-helix	20-25	6
α-helix	28-30	3
β-strand	36	1	99
α-helix	41-58	18
α-helix	63-66	4
α-helix	69-86	18
α-helix	94-96	3
α-helix	98-118	21
α-helix	122-126	5
α-helix	135-137	3
α-helix	138-181	44
α-helix	186-224	39

Chain AA: 21 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
β-strand	26	1	34
β-strand	29-33	5	35
β-strand	34	1	36
β-strand	38-43	6	35
α-helix	47	1
β-strand	48	1	37
β-strand	52-55	4	35
β-strand	60-66	7	35
β-strand	71-75	5	35
α-helix	79-81	3
β-strand	87-90	4	35
β-strand	96-98	3	38
β-strand	107-109	3	39
β-strand	114	1	39
β-strand	126-128	3	38
α-helix	131-134	4
β-strand	139	1	40
β-strand	145	1	41
α-helix	151-155	5
β-strand	160	1	41
β-strand	164	1	39
β-strand	166	1	42
β-strand	167-169	3	39
α-helix	175-185	11
α-helix	187-191	5
β-strand	199-206	8	39
α-helix	210-222	13
β-strand	230-234	5	39
α-helix	240-259	20
β-strand	263-269	7	39
α-helix	274-285	12
α-helix	291-293	3
α-helix	300-306	7
β-strand	312	1	40
β-strand	320-323	4	39
β-strand	326-328	3	39
α-helix	337-343	7
β-strand	348-349	2	42
β-strand	352	1	39
α-helix	354-358	5
β-strand	365	1	39
β-strand	371-372	2	42
α-helix	381-399	19
α-helix	401-403	3
α-helix	412-428	17
α-helix	438-449	12
α-helix	458-473	16
α-helix	477-485	9
α-helix	491-506	16

Chain Ab: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	2-6	5
β-strand	12-13	2	101
β-strand	17-18	2	101
α-helix	19-29	11
α-helix	32-47	16
α-helix	55-119	65
α-helix	120-122	3
α-helix	123-184	62
α-helix	190-208	19

Chain AB: 25 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	9-16	8
α-helix	19-21	3
β-strand	28-35	8	47
β-strand	38-43	6	47
α-helix	47	1
β-strand	48	1	48
β-strand	51	1	49
β-strand	52-54	3	47
β-strand	60-66	7	47
β-strand	71-75	5	47
α-helix	79-81	3
β-strand	87-89	3	47
β-strand	94	1	49
β-strand	96-99	4	50
β-strand	107-109	3	51
β-strand	114	1	51
β-strand	125-128	4	50
α-helix	131-134	4
β-strand	139	1	52
β-strand	145	1	53
α-helix	151-156	6
β-strand	160	1	53
β-strand	164	1	51
β-strand	167-168	2	54
α-helix	175-184	10
α-helix	185-187	3
β-strand	199-206	8	51
α-helix	210-221	12
β-strand	229-234	6	51
α-helix	240-258	19
β-strand	263-269	7	51
α-helix	271-284	14
α-helix	291-293	3
α-helix	300-306	7
β-strand	312	1	52
β-strand	320-323	4	51
β-strand	326-327	2	54
α-helix	337-343	7
β-strand	348	1	55
β-strand	350-352	3	54
α-helix	354-358	5
β-strand	365-366	2	54
β-strand	372	1	55
α-helix	375-377	3
α-helix	381-399	19
α-helix	400-402	3
α-helix	412-428	17
α-helix	438-449	12
α-helix	452-455	4
α-helix	458-460	3
α-helix	461-475	15
α-helix	477-486	10
α-helix	491-506	16

49 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 protein 8	8, A8	protein	66	Bos taurus	P03929 (AlphaFold model)
ATP synthase subunit alpha, mitochondrial	A, AA, AB, AC, B, C	protein	510	Bos taurus	P19483 (AlphaFold model)
ATP synthase subunit beta, mitochondrial	AD, AE, AF, D, E, F	protein	482	Bos taurus	P00829 (AlphaFold model)
ATP synthase subunit gamma, mitochondrial	AG, G	protein	273	Bos taurus	P05631 (AlphaFold model)
ATP synthase subunit delta, mitochondrial	AH, H	protein	146	Bos taurus	P05630
ATP synthase subunit epsilon, mitochondrial	AI, I	protein	50	Bos taurus	P05632
ATPase inhibitor, mitochondrial	AJ, J	protein	66	Bos taurus	P01096
ATP synthase F(0) complex subunit C2, mitochondrial	AK, AL, AM, AN, AO, AP, AQ, AR, K, L, M, N, O, P, Q, R	protein	75	Bos taurus	P07926
ATP synthase subunit O, mitochondrial	AS, S	protein	190	Bos taurus	P13621
ATP synthase subunit a	Aa, a	protein	226	Bos taurus	P00847
ATP synthase F(0) complex subunit B1, mitochondrial	Ab, b	protein	214	Bos taurus	P13619
ATP synthase subunit d, mitochondrial	Ad, d	protein	160	Bos taurus	P13620

6 more molecules are not listed.

Sequence of entity 1 (8, A8), FASTA

>7AJD_1 ATP synthase protein 8 (chains 8, A8)
MPQLDTSTWLTMILSMFLTLFIIFQLKVSKHNFYHNPELTPTKMLKQNTPWETKWTKIYL
PLLLPL

Sequence of entity 2 (A, AA, AB, AC, B, C), FASTA

>7AJD_2 ATP synthase subunit alpha, mitochondrial (chains A, AA, AB, AC, B, C)
EKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
GKIRTDGKISEESDAKLKEIVTNFLAGFEA

Sequence of entity 3 (AD, AE, AF, D, E, F), FASTA

>7AJD_3 ATP synthase subunit beta, mitochondrial (chains AD, AE, AF, D, E, F)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS

Sequence of entity 4 (AG, G), FASTA

>7AJD_4 ATP synthase subunit gamma, mitochondrial (chains AG, G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAALD

Sequence of entity 5 (AH, H), FASTA

>7AJD_5 ATP synthase subunit delta, mitochondrial (chains AH, H)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE

Sequence of entity 6 (AI, I), FASTA

>7AJD_6 ATP synthase subunit epsilon, mitochondrial (chains AI, I)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

Sequence of entity 7 (AJ, J), FASTA

>7AJD_7 ATPase inhibitor, mitochondrial (chains AJ, J)
GSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEI
HHHHHH

Sequence of entity 8 (AK, AL, AM, AN, AO, AP, AQ, AR, K, L, M, N, O, P, Q, R), FASTA

>7AJD_8 ATP synthase F(0) complex subunit C2, mitochondrial (chains AK, AL, AM, AN, AO, AP, AQ, AR, K, L, M, N, O, P, Q, R)
DIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAM
GLFCLMVAFLILFAM

Sequence of entity 9 (AS, S), FASTA

>7AJD_9 ATP synthase subunit O, mitochondrial (chains AS, S)
FAKLVRPPVQIYGIEGRYATALYSAASKQNKLEQVEKELLRVGQILKEPKMAASLLNPYV
KRSVKVKSLSDMTAKEKFSPLTSNLINLLAENGRLTNTPAVISAFSTMMSVHRGEVPCTV
TTASALDEATLTELKTVLKSFLSKGQVLKLEVKIDPSIMGGMIVRIGEKYVDMSAKTKIQ
KLSRAMREIL

Sequence of entity 10 (Aa, a), FASTA

>7AJD_10 ATP synthase subunit a (chains Aa, a)
MNENLFTSFITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSI
HNSKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNK
TKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLA
LMSISTTTALITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT

Sequence of entity 11 (Ab, b), FASTA

>7AJD_11 ATP synthase F(0) complex subunit B1, mitochondrial (chains Ab, b)
PVPPLPEHGGKVRFGLIPEEFFQFLYPKTGVTGPYVLGTGLILYLLSKEIYVITPETFSA
ISTIGFLVYIVKKYGASVGEFADKLNEQKIAQLEEVKQASIKQIQDAIDMEKSQQALVQK
RHYLFDVQRNNIAMALEVTYRERLHRVYREVKNRLDYHISVQNMMRQKEQEHMINWVEKR
VVQSISAQQEKETIAKCIADLKLLSKKAQAQPVM

Sequence of entity 12 (Ad, d), FASTA

>7AJD_12 ATP synthase subunit d, mitochondrial (chains Ad, d)
AGRKLALKTIDWVAFGEIIPRNQKAVANSLKSWNETLTSRLATLPEKPPAIDWAYYKANV
AKAGLVDDFEKKFNALKVPIPEDKYTAQVDAEEKEDVKSCAEFLTQSKTRIQEYEKELEK
MRNIIPFDQMTIEDLNEVFPETKLDKKKYPYWPHRPIETL

Ligands and cofactors

ID	Name	Formula	Copies
LHG	1,2-dipalmitoyl-phosphatidyl-glycerole	C38 H75 O10 P	4
CDL	Cardiolipin	C81 H156 O17 P2	6

Primary citation

Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes. Spikes, T.E., Montgomery, M.G., Walker, J.E. Proc Natl Acad Sci U S A (2021) 118. DOI 10.1073/pnas.2021012118 · 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)
9W2S 4.0 Å, Cryo-EM structure of FoF1-ATPase monomer state 3 on the bovine heart submitochondrial…
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

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