5ARI: Bovine mitochondrial ATP synthase state 2b

Bovine mitochondrial ATP synthase state 2b. Determined by electron microscopy at 7.4 Å resolution. Released 14 Oct 2015.

Method: Electron microscopy
Resolution: 7.4 Å
Organism: BOS TAURUS
Chains: 22
Atoms: 18,545
Mol. weight: 518.89 kDa
Released: 14 Oct 2015

Explore 5ARI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5ARI contains 220 α-helices and 154 β-strands across 22 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: 20 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
β-strand	8	1	1
α-helix	12-15	4
β-strand	28-35	8	2
β-strand	38-43	6	2
β-strand	51-55	5	2
β-strand	58-66	9	2
β-strand	70-75	6	2
β-strand	87-93	7	2
β-strand	97-99	3	3
β-strand	106-109	4	4
β-strand	114	1	4
β-strand	125-127	3	3
α-helix	132-134	3
β-strand	139	1	5
α-helix	151-156	6
β-strand	164	1	4
β-strand	166-170	5	4
α-helix	175-190	16
β-strand	199-205	7	4
α-helix	210-223	14
α-helix	225-228	4
β-strand	229-233	5	4
α-helix	240-258	19
β-strand	263-269	7	4
α-helix	271-284	14
α-helix	291-293	3
α-helix	298-307	10
β-strand	310-311	2	4
β-strand	312	1	5
α-helix	314-316	3
β-strand	320-329	10	4
α-helix	337-343	7
β-strand	349-351	3	4
α-helix	354-359	6
α-helix	375-378	4
α-helix	381-405	25
α-helix	412-428	17
α-helix	438-449	12
α-helix	458-474	17
α-helix	477-486	10
α-helix	491-508	18

Chain B: 19 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	28-34	7	2
β-strand	38-43	6	2
α-helix	47-48	2
β-strand	51-55	5	2
β-strand	58-66	9	2
β-strand	71-76	6	2
β-strand	87-93	7	2
β-strand	96-99	4	6
β-strand	107-110	4	7
β-strand	113-115	3	7
β-strand	125-128	4	6
β-strand	139	1	8
α-helix	151-156	6
β-strand	164	1	7
β-strand	166-169	4	7
α-helix	175-185	11
α-helix	187-190	4
β-strand	200-206	7	7
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	7
α-helix	240-258	19
β-strand	263-269	7	7
α-helix	271-284	14
α-helix	291-293	3
α-helix	298-307	10
β-strand	311	1	7
β-strand	312	1	8
α-helix	314-316	3
β-strand	320-328	9	7
α-helix	337-345	9
β-strand	348-351	4	7
α-helix	354-359	6
β-strand	371-372	2	7
α-helix	381-399	19
α-helix	412-428	17
α-helix	438-449	12
α-helix	459-474	16
α-helix	477-486	10
α-helix	491-506	16

Chain C: 18 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	25	1	9
β-strand	29-35	7	2
β-strand	38-43	6	2
β-strand	51-55	5	2
β-strand	60-66	7	2
β-strand	71-75	5	2
β-strand	87-94	8	2
β-strand	96-99	4	10
β-strand	106-109	4	11
β-strand	114	1	11
β-strand	125-128	4	10
β-strand	139	1	12
α-helix	151-156	6
β-strand	164	1	11
β-strand	166-169	4	11
α-helix	175-190	16
β-strand	199-205	7	11
α-helix	210-222	13
α-helix	225-228	4
β-strand	229-233	5	11
α-helix	240-259	20
β-strand	263-269	7	11
α-helix	271-284	14
α-helix	291-293	3
α-helix	298-307	10
β-strand	310-311	2	11
β-strand	312	1	12
α-helix	314-316	3
β-strand	320-328	9	11
β-strand	330	1	13
β-strand	333	1	13
α-helix	337-345	9
β-strand	348-352	5	11
α-helix	354-359	6
β-strand	365-372	8	11
α-helix	376-378	3
α-helix	381-402	22
α-helix	412-428	17
α-helix	438-449	12
α-helix	458-474	17
α-helix	477-486	10
α-helix	491-508	18

Chain D: 23 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	2
β-strand	19-25	7	2
α-helix	30-31	2
β-strand	35-38	4	2
β-strand	46-54	9	2
β-strand	57-62	6	2
β-strand	74-80	7	2
β-strand	84-85	2	14
α-helix	88-90	3
β-strand	91	1	15
β-strand	94-95	2	15
β-strand	113-114	2	14
α-helix	120-122	3
β-strand	126	1	16
β-strand	132-133	2	17
α-helix	134	1
α-helix	138-143	6
β-strand	146-147	2	17
β-strand	151-155	5	15
α-helix	162-169	8
α-helix	170-174	5
α-helix	175-176	2
β-strand	180-185	6	15
α-helix	190-203	14
β-strand	215-219	5	15
α-helix	226-241	16
α-helix	242-246	5
β-strand	250-256	7	15
α-helix	258-269	12
α-helix	278-280	3
α-helix	285-293	9
β-strand	299	1	16
β-strand	303-310	8	15
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-335	5	15
α-helix	337-341	5
β-strand	348-354	7	15
α-helix	364-381	18
α-helix	387-391	5
α-helix	400-414	15
α-helix	434-446	13
α-helix	463-473	11

Chain E: 20 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	2
β-strand	20-25	6	2
β-strand	35-39	5	2
β-strand	46-54	9	2
β-strand	57-62	6	2
β-strand	74-80	7	2
β-strand	84-86	3	18
α-helix	88-90	3
β-strand	94-96	3	19
β-strand	101	1	19
β-strand	112-114	3	18
α-helix	123-125	3
β-strand	129	1	20
α-helix	138-143	6
β-strand	148	1	20
β-strand	151-154	4	19
α-helix	162-177	16
β-strand	181-186	6	19
α-helix	190-203	14
β-strand	215-220	6	19
α-helix	226-241	16
α-helix	242-246	5
β-strand	251-256	6	19
α-helix	258-271	14
α-helix	278-280	3
α-helix	285-293	9
β-strand	298	1	21
β-strand	303	1	21
β-strand	304-309	6	19
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-333	3	19
β-strand	335	1	22
α-helix	337-341	5
β-strand	348	1	22
β-strand	354	1	19
α-helix	365-389	25
α-helix	398-414	17
α-helix	419-421	3
α-helix	434-446	13
α-helix	455-457	3
α-helix	464-471	8

Chain F: 22 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	2
β-strand	19-25	7	2
α-helix	30-31	2
β-strand	35-38	4	2
β-strand	46-54	9	2
β-strand	57-62	6	2
β-strand	74-80	7	2
β-strand	83-86	4	23
α-helix	88-90	3
β-strand	94-96	3	24
β-strand	101	1	24
β-strand	112-115	4	23
α-helix	123-125	3
β-strand	131-132	2	25
α-helix	133-134	2
α-helix	138-143	6
β-strand	147-148	2	25
β-strand	151-156	6	24
α-helix	162-169	8
α-helix	170-175	6
β-strand	180-186	7	24
α-helix	190-203	14
β-strand	215-220	6	24
α-helix	226-241	16
α-helix	242-246	5
β-strand	250-256	7	24
α-helix	259-271	13
α-helix	278-280	3
α-helix	285-293	9
β-strand	303-309	7	24
α-helix	313-315	3
α-helix	320-327	8
β-strand	331-335	5	24
α-helix	337-340	4
β-strand	348-355	8	24
α-helix	365-391	27
α-helix	393-395	3
α-helix	398-414	17
β-strand	418	1	26
α-helix	422-425	4
β-strand	427	1	26
α-helix	434-446	13
α-helix	463-472	10

Chain G: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	3-48	46
β-strand	70-71	2	27
α-helix	81-90	10
β-strand	106-108	3	27
α-helix	112-114	3
β-strand	126-128	3	27
β-strand	129	1	28
α-helix	138-150	13
β-strand	159-167	9	27
β-strand	170-177	8	27
β-strand	194	1	30
α-helix	198-265	68

Chain H: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	17-21	5	30
β-strand	26-32	7	30
β-strand	33-37	5	31
β-strand	40-41	2	30
β-strand	43	1	30
β-strand	46-48	3	31
β-strand	54-58	5	30
β-strand	61-67	7	31
β-strand	74-77	4	31
β-strand	80-84	5	30
β-strand	89-94	6	30
β-strand	97-99	3	31
α-helix	100-102	3
α-helix	105-120	16
α-helix	125-143	19

14 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, B, C	protein	510	BOS TAURUS	P19483 (AlphaFold model)
ATP synthase subunit beta, mitochondrial	D, E, F	protein	482	BOS TAURUS	P00829 (AlphaFold model)
ATP synthase subunit gamma, mitochondrial	G	protein	273	BOS TAURUS	P05631 (AlphaFold model)
ATP synthase subunit delta, mitochondrial	H	protein	146	BOS TAURUS	P05630 (AlphaFold model)
ATP synthase subunit epsilon, mitochondrial	I	protein	50	BOS TAURUS	P05632
ATP synthase F(0) complex subunit C1, mitochondrial	J, K, L, M, N, O, P, Q	protein	72	BOS TAURUS	P32876
ATP synthase subunit O, mitochondrial	S	protein	190	BOS TAURUS	P13621
ATP synthase F(0) complex subunit B1, mitochondrial	T	protein	174	BOS TAURUS	P13619
ATP synthase subunit D, mitochondrial	U	protein	124	BOS TAURUS	P13620
ATP synthase-coupling factor 6, mitochondrial	V	protein	77	BOS TAURUS	P02721
ATP synthase subunit beta, mitochondrial	W	protein	217	BOS TAURUS	P00847

Sequence of entity 1 (A, B, C), FASTA

>5ARI_1 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL (chains A, B, C)
QKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
GKIRTDGKISEESDAKLKEIVTNFLAGFEA

Sequence of entity 2 (D, E, F), FASTA

>5ARI_2 ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL (chains D, E, F)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS

Sequence of entity 3 (G), FASTA

>5ARI_3 ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL (chains G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAALD

Sequence of entity 4 (H), FASTA

>5ARI_4 ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL (chains H)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE

Sequence of entity 5 (I), FASTA

>5ARI_5 ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL (chains I)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

Sequence of entity 6 (J, K, L, M, N, O, P, Q), FASTA

>5ARI_6 ATP SYNTHASE F(0) COMPLEX SUBUNIT C1, MITOCHONDRIAL (chains J, K, L, M, N, O, P, Q)
IDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMG
LFCLMVAFLILF

Sequence of entity 7 (S), FASTA

>5ARI_7 ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL (chains S)
FAKLVRPPVQIYGIEGRYATALYSAASKQNKLEQVEKELLRVGQILKEPKMAASLLNPYV
KRSVKVKSLSDMTAKEKFSPLTSNLINLLAENGRLTNTPAVISAFSTMMSVHRGEVPCTV
TTASALDETTLTELKTVLKSFLSKGQVLKLEVKIDPSIMGGMIVRIGEKYVDMSAKTKIQ
KLSRAMREIL

Sequence of entity 8 (T), FASTA

>5ARI_8 ATP SYNTHASE F(0) COMPLEX SUBUNIT B1, MITOCHONDRIAL (chains T)
PYVLGTGLILYLLSKEIYVITPETFSAISTIGFLVYIVKKYGASVGEFADKLNEQKIAQL
EEVKQASIKQIQDAIDMEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLHRVYREVKN
RLDYHISVQNMMRQKEQEHMINWVEKRVVQSISAQQEKETIAKCIADLKLLSKK

Sequence of entity 9 (U), FASTA

>5ARI_9 ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL (chains U)
AGRKLALKTIDWVAFGEIIPRNQKAVANSLKSWNETLTSRLATLPEKPPAIDWAYYKANV
AKAGLVDDFEKKFNALKVPIPEDKYTAQVDAEEKEDVKSCAEFLTQSKTRIQEYEKELEK
MRNI

Sequence of entity 10 (V), FASTA

>5ARI_10 ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL (chains V)
FNKELDPVQKLFVDKIREYRTKRQTSGGPVDAGPEYQQDLDRELFKLKQMYGKADMNTFP
NFTFEDPKFEVVEKPQS

Sequence of entity 11 (W), FASTA

>5ARI_11 ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL (chains W)
ITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSIHNSKGQTWT
LMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNKTKASLAHFL
PQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLALMSISTTTA
LITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT

Primary citation

Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM. Zhou, A., Rohou, A., Schep, D.G. et al. Elife (2015) 4:e10180-e10180. DOI 10.7554/eLife.10180 · 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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