2V7Q: ATP synthase subunit alpha heart isoform

The structure of F1-ATPase inhibited by I1-60HIS, a monomeric form of the inhibitor protein, IF1. Determined by X-ray diffraction at 2.1 Å resolution. Released 18 Sept 2007.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: BOS TAURUS
Chains: 10
Atoms: 27,418
Mol. weight: 382.25 kDa
Ligands: ADP, MG, ATP, PO4
Released: 18 Sept 2007

Explore 2V7Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2V7Q contains 165 α-helices and 173 β-strands across 10 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, 28 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	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	3
α-helix	101-103	3
β-strand	107-108	2	4
β-strand	114	1	4
β-strand	125-128	4	3
α-helix	131-134	4
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	166-169	4	7
α-helix	175-185	11
α-helix	187-190	4
β-strand	200-206	7	4
α-helix	210-222	13
α-helix	226-228	3
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	298-306	9
β-strand	310-311	2	4
β-strand	312	1	5
α-helix	314-316	3
β-strand	320-325	6	4
β-strand	326-328	3	7
α-helix	337-345	9
β-strand	348-352	5	7
α-helix	354-359	6
β-strand	365	1	7
β-strand	371-372	2	7
α-helix	375-378	4
α-helix	381-397	17
α-helix	401-405	5
α-helix	412-427	16
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-475	15
α-helix	477-486	10
α-helix	491-506	16

Chain B: 26 helices, 29 β-strands

Element	Residues	Length	Sheet
β-strand	28-34	7	1
β-strand	39-43	5	1
α-helix	47	1
β-strand	48	1	9
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	10
α-helix	101-103	3
β-strand	107-108	2	11
β-strand	114	1	11
β-strand	125-128	4	10
α-helix	131-134	4
β-strand	139	1	12
β-strand	145-146	2	13
α-helix	151-156	6
β-strand	159-160	2	13
β-strand	164	1	11
β-strand	166-169	4	14
α-helix	175-185	11
α-helix	187-190	4
α-helix	195-197	3
β-strand	200-206	7	11
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	11
α-helix	240-258	19
β-strand	263-269	7	11
α-helix	271-284	14
β-strand	289	1	15
α-helix	291-293	3
β-strand	295	1	15
α-helix	298-306	9
β-strand	311	1	11
β-strand	312	1	12
α-helix	314-316	3
β-strand	320-325	6	11
β-strand	326-328	3	14
α-helix	337-343	7
β-strand	348-351	4	14
β-strand	352	1	16
α-helix	354-359	6
β-strand	365	1	16
β-strand	371-372	2	14
α-helix	375-378	4
α-helix	381-390	10
α-helix	392-399	8
α-helix	413-427	15
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-474	14
α-helix	477-486	10
α-helix	491-505	15

Chain C: 24 helices, 29 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	17
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	18
α-helix	101-103	3
β-strand	107-108	2	19
β-strand	114	1	19
β-strand	125-128	4	18
α-helix	131-134	4
β-strand	139	1	20
β-strand	145-146	2	21
α-helix	151-156	6
β-strand	159-160	2	21
β-strand	164	1	19
β-strand	165-169	5	22
α-helix	175-185	11
α-helix	187-190	4
α-helix	195-197	3
β-strand	200-206	7	19
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	19
α-helix	240-259	20
β-strand	263-269	7	19
α-helix	271-284	14
α-helix	287-289	3
α-helix	291-293	3
α-helix	298-306	9
β-strand	310-311	2	19
β-strand	312	1	20
α-helix	314-316	3
β-strand	320-325	6	19
β-strand	326-328	3	22
α-helix	337-345	9
β-strand	348-351	4	22
β-strand	352	1	23
α-helix	354-359	6
β-strand	365	1	23
β-strand	371	1	22
β-strand	378	1	24
β-strand	380	1	24
α-helix	382-398	17
α-helix	401-403	3
α-helix	419-427	9
α-helix	438-449	12
α-helix	461-475	15
α-helix	496-508	13

Chain D: 25 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	1
β-strand	20-25	6	1
α-helix	28-31	4
β-strand	34-38	5	1
β-strand	46-54	9	1
β-strand	57-62	6	1
β-strand	70	1	17
β-strand	74-81	8	1
β-strand	83-85	3	25
α-helix	88-90	3
β-strand	94-95	2	26
β-strand	101	1	26
β-strand	113-115	3	25
α-helix	119-122	4
α-helix	123-125	3
β-strand	132-133	2	27
α-helix	138-143	6
β-strand	146-147	2	27
β-strand	151-156	6	26
α-helix	162-169	8
α-helix	170-174	5
β-strand	180-186	7	26
α-helix	190-202	13
β-strand	215-220	6	26
α-helix	226-246	21
β-strand	251-256	6	26
α-helix	259-269	11
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	299	1	28
β-strand	302	1	28
β-strand	304-311	8	26
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	26
β-strand	335	1	29
α-helix	337-341	5
β-strand	348	1	29
β-strand	354-355	2	26
α-helix	360-363	4
α-helix	365-391	27
α-helix	398-413	16
α-helix	419-421	3
α-helix	427-429	3
α-helix	434-446	13
α-helix	454-457	4
α-helix	463-475	13

Chain E: 24 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	11-17	7	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	2
β-strand	74-77	4	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	118-122	5
α-helix	123-125	3
β-strand	132-133	2	32
α-helix	138-143	6
β-strand	146-147	2	32
β-strand	151-155	5	31
α-helix	162-176	15
β-strand	181-186	6	31
α-helix	190-203	14
β-strand	215-220	6	31
α-helix	226-246	21
β-strand	250-256	7	31
α-helix	258-271	14
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	298	1	31
β-strand	303-309	7	31
α-helix	313-315	3
α-helix	320-326	7
β-strand	331-334	4	31
β-strand	335	1	33
α-helix	337-341	5
β-strand	348	1	33
β-strand	354-355	2	31
α-helix	360-363	4
α-helix	365-388	24
α-helix	393-395	3
α-helix	398-412	15
α-helix	419-421	3
α-helix	422-425	4
α-helix	434-445	12
α-helix	454-456	3
α-helix	463-472	10

Chain F: 24 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	34-38	5	1
β-strand	46-54	9	1
β-strand	57-62	6	1
β-strand	70	1	9
β-strand	74-81	8	1
β-strand	83-86	4	34
α-helix	88-90	3
β-strand	91	1	35
β-strand	94-95	2	35
β-strand	101	1	35
β-strand	112-115	4	34
α-helix	123-125	3
β-strand	132-133	2	36
α-helix	138-143	6
β-strand	146-147	2	36
β-strand	151-156	6	35
α-helix	162-173	12
β-strand	180-186	7	35
α-helix	190-203	14
β-strand	215-220	6	35
α-helix	226-245	20
β-strand	251-256	6	35
α-helix	259-272	14
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	304-311	8	35
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	35
β-strand	335	1	37
α-helix	337-340	4
β-strand	348	1	37
β-strand	354-355	2	35
α-helix	360-363	4
α-helix	365-391	27
α-helix	393-395	3
α-helix	398-413	16
α-helix	419-421	3
α-helix	422-425	4
α-helix	434-445	12
α-helix	454-457	4
α-helix	464-471	8

Chain G: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	3-48	46
α-helix	52-54	3
β-strand	66-71	6	38
α-helix	81-95	15
β-strand	103-108	6	38
α-helix	110-120	11
α-helix	121-123	3
β-strand	124-129	6	38
α-helix	138-149	12
β-strand	157-165	9	38
β-strand	171-177	7	38
α-helix	190-192	3
α-helix	198-271	74

Chain H: 4 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	39
β-strand	26-40	15	39
β-strand	43-48	6	39
α-helix	51-53	3
β-strand	54-58	5	39
β-strand	61-67	7	39
β-strand	72-77	6	39
β-strand	80-84	5	39
β-strand	90-94	5	39
β-strand	97-98	2	39
α-helix	100-102	3
β-strand	103	1	40
α-helix	105-119	15
α-helix	125-144	20

2 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 heart isoform	A, B, C	protein	510	BOS TAURUS	P19483 (AlphaFold model)
ATP synthase subunit beta	D, E, F	protein	482	BOS TAURUS	P00829 (AlphaFold model)
ATP synthase gamma chain	G	protein	272	BOS TAURUS	P05631 (AlphaFold model)
ATP synthase delta chain	H	protein	146	BOS TAURUS	P05630 (AlphaFold model)
ATP synthase epsilon chain	I	protein	50	BOS TAURUS	P05632
Atpase inhibitor	J	protein	66	BOS TAURUS	P01096

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

>2V7Q_1 ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM (chains A, B, C)
EKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
SKIRTDGKISEESDAKLKEIVTNFLAGFEA

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

>2V7Q_2 ATP SYNTHASE SUBUNIT BETA (chains D, E, F)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS

Sequence of entity 3 (G), FASTA

>2V7Q_3 ATP SYNTHASE GAMMA CHAIN (chains G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAAL

Sequence of entity 4 (H), FASTA

>2V7Q_4 ATP SYNTHASE DELTA CHAIN (chains H)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE

Sequence of entity 5 (I), FASTA

>2V7Q_5 ATP SYNTHASE EPSILON CHAIN (chains I)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

Sequence of entity 6 (J), FASTA

>2V7Q_6 ATPASE INHIBITOR (chains J)
GSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEI
HHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2
MG	Magnesium ion	Mg	5
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	3
PO4	Phosphate ion	O4 P	1

Primary citation

How the Regulatory Protein, If1, Inhibits F1- ATPase from Bovine Mitochondria. Gledhill, J.R., Montgomery, M.G., Leslie, A.G.W. et al. Proc Natl Acad Sci U S A (2007) 104:15671. DOI 10.1073/PNAS.0707326104 · 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)
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
2JJ1 2.7 Å, The Structure of F1-ATPase inhibited by piceatannol.

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