7AJF: Bovine ATP synthase dimer state2:state2

bovine ATP synthase dimer state2:state2. Determined by electron microscopy at 8.45 Å resolution. Released 3 Feb 2021.

Method: Electron microscopy
Resolution: 8.45 Å
Organism: Bos taurus
Chains: 58
Atoms: 51,354
Mol. weight: 1195.4 kDa
Ligands: CDL, LHG
Released: 3 Feb 2021

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

Secondary structure: helices and β-sheets

7AJF contains 503 α-helices and 387 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: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	2-4	3
α-helix	6-18	13
α-helix	19-23	5
α-helix	24-29	6
α-helix	34-37	4

Chain a: 12 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	3-9	7
α-helix	11-12	2
β-strand	15	1	140
β-strand	17	1	140
α-helix	19-25	7
α-helix	26-30	5
β-strand	36	1	141
α-helix	41-57	17
α-helix	58-60	3
α-helix	63-86	24
α-helix	98-105	8
α-helix	107-128	22
α-helix	135-137	3
α-helix	138-181	44
α-helix	186-224	39

Chain A: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	29-31	3	1
β-strand	38-40	3	2
β-strand	41-43	3	1
α-helix	48	1
β-strand	51-53	3	2
β-strand	61-66	6	2
β-strand	71-74	4	2
β-strand	96-97	2	3
α-helix	101-103	3
β-strand	104	1	4
β-strand	108	1	5
β-strand	114	1	5
β-strand	127-128	2	3
α-helix	131-134	4
β-strand	139-140	2	6
α-helix	144-146	3
α-helix	151-156	6
β-strand	164	1	6
β-strand	168-169	2	7
α-helix	175-191	17
β-strand	199	1	8
β-strand	201-208	8	4
α-helix	210-222	13
α-helix	225-227	3
β-strand	229-235	7	4
α-helix	240-259	20
β-strand	263	1	8
β-strand	264-266	3	6
α-helix	272-284	13
α-helix	291-293	3
α-helix	296-298	3
α-helix	300-306	7
β-strand	310-312	3	6
β-strand	320-323	4	6
β-strand	327-328	2	7
α-helix	337-345	9
β-strand	349	1	9
β-strand	352	1	10
α-helix	354-358	5
β-strand	365	1	10
β-strand	371	1	9
α-helix	381-404	24
α-helix	412-428	17
α-helix	438-449	12
α-helix	458-471	14
α-helix	472-476	5
α-helix	477-486	10
α-helix	491-506	16

Chain A8: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	2-4	3
α-helix	6-18	13
α-helix	19-24	6
α-helix	25-28	4

Chain Aa: 13 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	3-8	6
α-helix	11-12	2
α-helix	19-22	4
α-helix	23-25	3
α-helix	27-30	4
β-strand	36	1	145
α-helix	41-60	20
α-helix	66-85	20
α-helix	94-96	3
α-helix	98-119	22
α-helix	121-126	6
α-helix	135-137	3
α-helix	138-181	44
α-helix	186-224	39

Chain AA: 26 helices, 30 β-strands

Element	Residues	Length	Sheet
β-strand	31	1	32
β-strand	33	1	33
β-strand	34-35	2	34
β-strand	40	1	33
β-strand	41	1	35
α-helix	47-48	2
β-strand	51-54	4	36
β-strand	60-62	3	37
β-strand	71	1	35
β-strand	74-76	3	37
β-strand	86	1	32
β-strand	89-94	6	36
β-strand	96-98	3	38
α-helix	101-103	3
β-strand	126-128	3	38
β-strand	139-140	2	39
β-strand	146	1	40
α-helix	151-155	5
β-strand	159	1	40
β-strand	164	1	41
β-strand	168-169	2	42
α-helix	177-179	3
α-helix	180-188	9
β-strand	201-205	5	41
α-helix	210-222	13
β-strand	229-233	5	41
α-helix	240-245	6
α-helix	247-249	3
α-helix	250-258	9
β-strand	263-269	7	41
α-helix	271-273	3
α-helix	274-284	11
α-helix	291-293	3
α-helix	297-306	10
β-strand	311-312	2	39
α-helix	314-316	3
β-strand	320-325	6	41
β-strand	327-328	2	42
α-helix	330-332	3
α-helix	337-344	8
β-strand	349	1	43
β-strand	352	1	44
α-helix	354-358	5
β-strand	365	1	44
β-strand	371	1	43
α-helix	381-386	6
α-helix	390-398	9
α-helix	401-406	6
α-helix	412-425	14
β-strand	431	1	45
β-strand	434	1	45
α-helix	438-450	13
α-helix	452-455	4
α-helix	458-472	15
α-helix	477-485	9
α-helix	491-506	16

Chain Ab: 11 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	10-11	2
β-strand	12-13	2	146
β-strand	17-18	2	146
α-helix	21-29	9
α-helix	32-36	5
α-helix	41-47	7
α-helix	57-70	14
α-helix	71-75	5
α-helix	78-125	48
α-helix	128-173	46
α-helix	176-185	10
α-helix	190-208	19

Chain AB: 27 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	11-16	6
β-strand	28-35	8	54
β-strand	38-43	6	54
α-helix	48	1
β-strand	51	1	55
β-strand	61-65	5	56
β-strand	72-75	4	56
α-helix	79-81	3
β-strand	87-89	3	54
β-strand	94	1	55
β-strand	96-99	4	57
β-strand	107-108	2	58
β-strand	125-128	4	57
α-helix	144	1
β-strand	145	1	59
α-helix	146-147	2
α-helix	153-156	4
β-strand	160	1	59
β-strand	167	1	60
α-helix	175-178	4
α-helix	180-188	9
β-strand	201	1	61
β-strand	202	1	62
α-helix	210-223	14
β-strand	230	1	62
β-strand	231-232	2	58
α-helix	240-250	11
α-helix	252-259	8
β-strand	264-265	2	61
β-strand	268	1	63
α-helix	271-285	15
α-helix	291-293	3
α-helix	296-306	11
α-helix	314-316	3
β-strand	321-322	2	61
β-strand	325	1	63
α-helix	337-345	9
β-strand	348	1	64
β-strand	350	1	60
β-strand	352	1	65
α-helix	354-358	5
β-strand	365	1	65
β-strand	372	1	64
α-helix	381-385	5
α-helix	388-400	13
α-helix	412-415	4
α-helix	416-420	5
α-helix	421-426	6
α-helix	438-449	12
α-helix	458-468	11
α-helix	470-474	5
α-helix	477-484	8
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 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 (AlphaFold model)
ATP synthase subunit epsilon, mitochondrial	AI, I	protein	50	Bos taurus	P05632
ATPase inhibitor, mitochondrial	AJ, J	protein	84	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
ATP synthase subunit e, mitochondrial	Ae, e	protein	70	Bos taurus	Q00361

6 more molecules are not listed.

Sequence of entity 1 (A, AA, AB, AC, B, C), FASTA

>7AJF_1 ATP synthase subunit alpha, mitochondrial (chains A, AA, AB, AC, B, C)
EKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
GKIRTDGKISEESDAKLKEIVTNFLAGFEA

Sequence of entity 2 (AD, AE, AF, D, E, F), FASTA

>7AJF_2 ATP synthase subunit beta, mitochondrial (chains AD, AE, AF, D, E, F)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS

Sequence of entity 3 (AG, G), FASTA

>7AJF_3 ATP synthase subunit gamma, mitochondrial (chains AG, G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAALD

Sequence of entity 4 (AH, H), FASTA

>7AJF_4 ATP synthase subunit delta, mitochondrial (chains AH, H)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE

Sequence of entity 5 (AI, I), FASTA

>7AJF_5 ATP synthase subunit epsilon, mitochondrial (chains AI, I)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

Sequence of entity 6 (AJ, J), FASTA

>7AJF_6 ATPase inhibitor, mitochondrial (chains AJ, J)
GSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEI
ERLQKEIERHKQSIKKLKQSEDDD

Sequence of entity 7 (AK, AL, AM, AN, AO, AP, AQ, AR, K, L, M, N, O, P, Q, R), FASTA

>7AJF_7 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 8 (AS, S), FASTA

>7AJF_8 ATP synthase subunit O, mitochondrial (chains AS, S)
FAKLVRPPVQIYGIEGRYATALYSAASKQNKLEQVEKELLRVGQILKEPKMAASLLNPYV
KRSVKVKSLSDMTAKEKFSPLTSNLINLLAENGRLTNTPAVISAFSTMMSVHRGEVPCTV
TTASALDEATLTELKTVLKSFLSKGQVLKLEVKIDPSIMGGMIVRIGEKYVDMSAKTKIQ
KLSRAMREIL

Sequence of entity 9 (Aa, a), FASTA

>7AJF_9 ATP synthase subunit a (chains Aa, a)
MNENLFTSFITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSI
HNSKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNK
TKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLA
LMSISTTTALITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT

Sequence of entity 10 (Ab, b), FASTA

>7AJF_10 ATP synthase F(0) complex subunit B1, mitochondrial (chains Ab, b)
PVPPLPEHGGKVRFGLIPEEFFQFLYPKTGVTGPYVLGTGLILYLLSKEIYVITPETFSA
ISTIGFLVYIVKKYGASVGEFADKLNEQKIAQLEEVKQASIKQIQDAIDMEKSQQALVQK
RHYLFDVQRNNIAMALEVTYRERLHRVYREVKNRLDYHISVQNMMRQKEQEHMINWVEKR
VVQSISAQQEKETIAKCIADLKLLSKKAQAQPVM

Sequence of entity 11 (Ad, d), FASTA

>7AJF_11 ATP synthase subunit d, mitochondrial (chains Ad, d)
AGRKLALKTIDWVAFGEIIPRNQKAVANSLKSWNETLTSRLATLPEKPPAIDWAYYKANV
AKAGLVDDFEKKFNALKVPIPEDKYTAQVDAEEKEDVKSCAEFLTQSKTRIQEYEKELEK
MRNIIPFDQMTIEDLNEVFPETKLDKKKYPYWPHRPIETL

Sequence of entity 12 (Ae, e), FASTA

>7AJF_12 ATP synthase subunit e, mitochondrial (chains Ae, e)
VPPVQVSPLIKLGRYSALFLGMAYGAKRYNYLKPRAEEERRLAAEEKKKRDEQKRIEREL
AEAQEDTILK

Ligands and cofactors

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

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 P19483 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2JDI 1.9 Å, Ground state structure of F1-ATPase from bovine heart mitochondria (Bovine F1-ATPase…
2CK3 1.95 Å, Azide inhibited bovine F1-ATPase
1H8E 2.0 Å, (ADP.AlF4)2(ADP.SO4) bovine F1-ATPase (all three catalytic sites occupied)
2V7Q 2.1 Å, The structure of F1-ATPase inhibited by I1-60HIS, a monomeric form of the inhibitor…
1W0J 2.2 Å, Beryllium fluoride inhibited bovine F1-ATPase
2JIZ 2.3 Å, The Structure of F1-ATPase inhibited by resveratrol.
9VPD 2.3 Å, Cryo-EM structure of the IF1 bound bovine ATP synthase monomer: rotary state 1, F1…
1E79 2.4 Å, Bovine F1-ATPase inhibited by DCCD (dicyclohexylcarbodiimide)
2JJ2 2.4 Å, The Structure of F1-ATPase inhibited by quercetin.
1E1R 2.5 Å, Bovine mitochondrial F1-atpase inhibited by MG2+ADP and aluminium fluoride
4ASU 2.6 Å, F1-ATPase in which all three catalytic sites contain bound nucleotide, with magnesium…
1E1Q 2.61 Å, Bovine mitochondrial F1-atpase at 100K

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