4ASU: ATP synthase subunit alpha, mitochondrial

F1-ATPase in which all three catalytic sites contain bound nucleotide, with magnesium ion released in the Empty site. Determined by X-ray diffraction at 2.6 Å resolution. Released 27 Jun 2012.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: BOS TAURUS
Chains: 9
Atoms: 24,283
Mol. weight: 374.47 kDa
Ligands: MG, ADP
Released: 27 Jun 2012

Explore 4ASU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4ASU contains 153 α-helices and 172 β-strands across 9 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: 26 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	71-76	6	1
α-helix	79-81	3
β-strand	87-90	4	1
β-strand	96-99	4	2
α-helix	101-103	3
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	1	5
α-helix	151-156	6
β-strand	160	1	5
β-strand	164	1	3
β-strand	165-169	5	6
α-helix	175-185	11
α-helix	187-190	4
β-strand	200-206	7	3
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	3
α-helix	240-259	20
β-strand	263-269	7	3
α-helix	271-284	14
α-helix	287-288	2
β-strand	289	1	7
α-helix	291-293	3
β-strand	295	1	7
α-helix	298-306	9
β-strand	311	1	3
β-strand	312	1	4
α-helix	314-316	3
β-strand	320-325	6	3
β-strand	326-328	3	6
α-helix	337-345	9
β-strand	348-352	5	6
α-helix	354-359	6
β-strand	365	1	6
β-strand	371-372	2	6
α-helix	375-377	3
α-helix	381-398	18
α-helix	401-403	3
α-helix	412-428	17
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-475	15
α-helix	477-486	10
α-helix	491-508	18

Chain B: 26 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	28-34	7	1
β-strand	38-43	6	1
α-helix	47	1
β-strand	48	1	8
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	96-98	3	9
α-helix	101-103	3
β-strand	107-108	2	10
β-strand	114	1	10
β-strand	126-128	3	9
α-helix	131-134	4
β-strand	139	1	11
β-strand	145	1	12
α-helix	151-156	6
β-strand	160	1	12
β-strand	164	1	10
β-strand	166-169	4	13
α-helix	175-185	11
α-helix	187-190	4
α-helix	195-197	3
β-strand	200-206	7	10
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	10
α-helix	240-258	19
β-strand	263-269	7	10
α-helix	271-284	14
α-helix	287-288	2
β-strand	289	1	14
α-helix	291-293	3
β-strand	295	1	14
α-helix	298-306	9
β-strand	311	1	10
β-strand	312	1	11
α-helix	314-316	3
β-strand	320-325	6	10
β-strand	326-328	3	13
α-helix	337-343	7
β-strand	348-351	4	13
β-strand	352	1	15
α-helix	354-359	6
β-strand	365	1	15
β-strand	371-372	2	13
α-helix	381-398	18
α-helix	412-427	16
α-helix	435-437	3
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-475	15
α-helix	477-486	10
α-helix	491-507	17

Chain C: 25 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	28-35	8	1
β-strand	38-43	6	1
α-helix	47	1
β-strand	48	1	16
β-strand	52-54	3	1
β-strand	60-66	7	1
β-strand	71-75	5	1
β-strand	87-90	4	1
β-strand	96-99	4	17
α-helix	101-103	3
β-strand	107-108	2	18
β-strand	114	1	18
β-strand	125-128	4	17
α-helix	131-134	4
β-strand	139	1	19
β-strand	145	1	20
α-helix	151-156	6
β-strand	160	1	20
β-strand	164	1	18
β-strand	166-169	4	21
α-helix	175-185	11
α-helix	187-190	4
β-strand	200-206	7	18
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	18
α-helix	240-258	19
β-strand	263-269	7	18
α-helix	271-284	14
α-helix	287-289	3
α-helix	291-293	3
α-helix	298-306	9
β-strand	311	1	18
β-strand	312	1	19
α-helix	314-316	3
β-strand	320-325	6	18
β-strand	326-328	3	21
α-helix	337-345	9
β-strand	348-352	5	21
α-helix	354-358	5
β-strand	365	1	21
β-strand	371-372	2	21
α-helix	375-378	4
α-helix	381-401	21
α-helix	412-427	16
α-helix	435-437	3
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-475	15
α-helix	477-486	10
α-helix	491-509	19

Chain D: 24 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	1
β-strand	20-24	5	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	70	1	16
β-strand	74-77	4	1
β-strand	83-85	3	22
α-helix	88-90	3
β-strand	91	1	23
β-strand	94-95	2	23
β-strand	101	1	23
β-strand	113-115	3	22
α-helix	119-122	4
α-helix	123-125	3
β-strand	126	1	24
β-strand	132-133	2	25
α-helix	138-142	5
β-strand	146-147	2	25
β-strand	151-156	6	23
α-helix	162-173	12
β-strand	180-186	7	23
α-helix	190-203	14
β-strand	215-220	6	23
α-helix	226-245	20
β-strand	251-256	6	23
α-helix	259-269	11
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	299	1	24
β-strand	304-311	8	23
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	23
β-strand	335	1	26
α-helix	337-342	6
β-strand	348	1	26
α-helix	365-385	21
α-helix	393-395	3
α-helix	398-413	16
α-helix	422-425	4
α-helix	428-429	2
α-helix	434-446	13
α-helix	454-456	3
α-helix	463-472	10

Chain E: 22 helices, 22 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	74-77	4	1
β-strand	83-86	4	27
α-helix	88-90	3
β-strand	94-95	2	28
β-strand	101	1	28
β-strand	112-115	4	27
α-helix	119-122	4
α-helix	123-125	3
β-strand	132-133	2	29
α-helix	138-143	6
α-helix	145	1
β-strand	146-147	2	29
β-strand	151-155	5	28
α-helix	162-176	15
β-strand	181-186	6	28
α-helix	190-203	14
β-strand	215-220	6	28
α-helix	226-245	20
β-strand	250-256	7	28
α-helix	258-271	14
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	298	1	28
β-strand	303-309	7	28
α-helix	313-315	3
α-helix	320-326	7
β-strand	331-334	4	28
β-strand	335	1	30
α-helix	337-341	5
β-strand	348	1	30
β-strand	355	1	28
α-helix	367-383	17
α-helix	398-414	17
α-helix	428-429	2
α-helix	434-446	13
α-helix	454-456	3
α-helix	464-472	9

Chain F: 23 helices, 24 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	34-38	5	1
β-strand	46-54	9	1
β-strand	57-62	6	1
β-strand	70	1	8
β-strand	74-81	8	1
β-strand	83-86	4	31
α-helix	88-90	3
β-strand	94-95	2	32
β-strand	101	1	32
β-strand	112-115	4	31
α-helix	119-122	4
α-helix	123-125	3
β-strand	126	1	33
β-strand	132-133	2	34
α-helix	138-143	6
β-strand	146-147	2	34
β-strand	151-156	6	32
α-helix	162-173	12
β-strand	180-186	7	32
α-helix	190-203	14
β-strand	215-220	6	32
α-helix	226-245	20
β-strand	251-256	6	32
α-helix	259-269	11
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	299	1	33
β-strand	304-311	8	32
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	32
β-strand	335	1	35
α-helix	337-341	5
β-strand	348	1	35
β-strand	355	1	32
α-helix	360-363	4
α-helix	365-390	26
α-helix	393-395	3
α-helix	398-414	17
α-helix	434-446	13
α-helix	454-456	3
α-helix	463-472	10

Chain G: 6 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	3-36	34
α-helix	39-42	4
β-strand	70	1	36
β-strand	71	1	37
β-strand	108	1	37
β-strand	128-129	2	37
α-helix	135-137	3
α-helix	138-147	10
β-strand	161	1	36
α-helix	163	1
β-strand	164-165	2	38
β-strand	171-172	2	38
α-helix	207-269	63

Chain H: 0 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	19-21	3	39
β-strand	26-28	3	39
β-strand	35-39	5	40
β-strand	40	1	41
β-strand	44-48	5	40
β-strand	54-57	4	39
β-strand	58	1	41
β-strand	61-66	6	40
β-strand	72-77	6	40
β-strand	80-84	5	39
β-strand	90-94	5	39
β-strand	97-98	2	40

1 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	480	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

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

>4ASU_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

>4ASU_2 ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL (chains D, E, F)
QASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTV
RTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAIHA
EAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHG
GYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLT
VAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITT
TKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIM
DPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPF
QVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHS

Sequence of entity 3 (G), FASTA

>4ASU_3 ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL (chains G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAALD

Sequence of entity 4 (H), FASTA

>4ASU_4 ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL (chains H)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE

Sequence of entity 5 (I), FASTA

>4ASU_5 ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL (chains I)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	5
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	6

Primary citation

Structural Evidence of a New Catalytic Intermediate in the Pathway of ATP Hydrolysis by F1-ATPase from Bovine Heart Mitochondria. Rees, D.M., Montgomery, M.G., Leslie, A.G. et al. Proc Natl Acad Sci U S A (2012) 109:11139. DOI 10.1073/PNAS.1207587109 · 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
1E1Q 2.61 Å, Bovine mitochondrial F1-atpase at 100K
2JJ1 2.7 Å, The Structure of F1-ATPase inhibited by piceatannol.

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