1OHH: BOVINE MITOCHONDRIAL F1-ATPASE

BOVINE MITOCHONDRIAL F1-ATPASE complexed with the inhibitor protein IF1. Determined by X-ray diffraction at 2.8 Å resolution. Released 9 Jun 2003.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Bos taurus
Chains: 8
Atoms: 22,859
Mol. weight: 363.62 kDa
Ligands: MG, ANP
Released: 9 Jun 2003

Explore 1OHH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OHH contains 153 α-helices and 151 β-strands across 8 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: 24 helices, 29 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
β-strand	87-90	4	1
β-strand	96-98	3	2
α-helix	101-103	3
β-strand	107-108	2	3
β-strand	114	1	3
β-strand	126-128	3	2
α-helix	132-134	3
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	199-206	8	3
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	3
α-helix	240-258	19
β-strand	263-269	7	3
α-helix	271-285	15
β-strand	289	1	7
α-helix	291-293	3
β-strand	295	1	7
α-helix	298-307	10
β-strand	310-311	2	3
β-strand	312	1	4
α-helix	314-316	3
β-strand	320-325	6	3
β-strand	326-328	3	6
β-strand	330	1	8
β-strand	333	1	8
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	375-378	4
α-helix	381-400	20
α-helix	403-406	4
α-helix	412-428	17
α-helix	438-449	12
α-helix	452-454	3
α-helix	458-475	18
α-helix	477-485	9
α-helix	493-508	16

Chain B: 24 helices, 24 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	51-54	4	1
β-strand	60-67	8	1
β-strand	70-75	6	1
α-helix	79-81	3
β-strand	87-94	8	1
β-strand	96-99	4	9
α-helix	101-103	3
β-strand	106-109	4	10
β-strand	114	1	10
β-strand	125-128	4	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	175-190	16
β-strand	200-206	7	10
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	10
α-helix	240-259	20
β-strand	263-269	7	10
α-helix	272-284	13
α-helix	287-289	3
α-helix	291-293	3
α-helix	298-307	10
β-strand	311	1	10
β-strand	312	1	11
α-helix	314-316	3
β-strand	320-323	4	10
β-strand	326-328	3	13
α-helix	337-343	7
β-strand	349-352	4	13
α-helix	354-357	4
β-strand	365	1	13
α-helix	375-378	4
α-helix	381-400	20
α-helix	412-427	16
α-helix	435-437	3
α-helix	438-450	13
α-helix	458-475	18
α-helix	477-486	10
α-helix	491-505	15

Chain C: 27 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	51-55	5	1
β-strand	60-67	8	1
β-strand	70-75	6	1
β-strand	87-94	8	1
β-strand	96-99	4	14
α-helix	101-103	3
β-strand	107-108	2	15
β-strand	114	1	15
β-strand	125-128	4	14
α-helix	131-134	4
β-strand	139	1	16
β-strand	145-146	2	17
α-helix	151	1
α-helix	152-156	5
β-strand	159-160	2	17
β-strand	164	1	15
β-strand	167-169	3	18
α-helix	175-185	11
α-helix	187-191	5
α-helix	195-197	3
β-strand	199-208	10	15
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-235	7	15
α-helix	240-258	19
β-strand	263-269	7	15
α-helix	271-283	13
α-helix	291-293	3
α-helix	298-306	9
β-strand	310-311	2	15
β-strand	312	1	16
α-helix	314-316	3
β-strand	320-323	4	15
β-strand	326-328	3	18
α-helix	337-343	7
β-strand	348-349	2	19
β-strand	350-351	2	18
β-strand	352	1	20
α-helix	354-359	6
β-strand	365	1	20
α-helix	367-369	3
β-strand	371-372	2	19
α-helix	375-378	4
α-helix	381-386	6
α-helix	390-401	12
α-helix	412-428	17
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-475	15
α-helix	477-485	9
α-helix	491-508	18

Chain D: 24 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	35-38	4	1
β-strand	46-54	9	1
β-strand	57-62	6	1
β-strand	74-77	4	1
β-strand	83-85	3	21
α-helix	88-90	3
β-strand	94-95	2	22
β-strand	101	1	22
β-strand	113-115	3	21
α-helix	119-122	4
β-strand	126	1	23
β-strand	132-133	2	24
α-helix	138-143	6
β-strand	146-147	2	24
β-strand	151-156	6	22
α-helix	162-169	8
α-helix	170-174	5
β-strand	180-186	7	22
α-helix	190-203	14
β-strand	215-220	6	22
α-helix	226-245	20
β-strand	251-256	6	22
α-helix	259-266	8
α-helix	270-272	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	299	1	23
β-strand	302	1	23
β-strand	304-311	8	22
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	22
β-strand	335	1	25
α-helix	337-341	5
β-strand	348	1	25
β-strand	355	1	22
α-helix	360-391	32
α-helix	400-413	14
α-helix	419-421	3
α-helix	422-425	4
α-helix	434-446	13
α-helix	448-451	4
α-helix	454-457	4
α-helix	463-476	14

Chain E: 21 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	74-81	8	1
β-strand	83-86	4	26
α-helix	88-90	3
β-strand	94-95	2	27
β-strand	101	1	27
β-strand	112-115	4	26
α-helix	119-122	4
β-strand	126	1	28
β-strand	132-133	2	29
α-helix	138-143	6
β-strand	146-147	2	29
β-strand	151-155	5	27
α-helix	162-177	16
β-strand	181-186	6	27
α-helix	190-201	12
β-strand	215-220	6	27
α-helix	226-245	20
β-strand	250-256	7	27
α-helix	259-271	13
α-helix	278-280	3
α-helix	285-293	9
β-strand	298	1	27
β-strand	299	1	28
β-strand	303-309	7	27
α-helix	313-315	3
α-helix	320-325	6
β-strand	329-334	6	27
β-strand	335	1	30
α-helix	337-341	5
β-strand	348	1	30
β-strand	354-355	2	27
α-helix	360-363	4
α-helix	365-387	23
α-helix	388-392	5
α-helix	398-413	16
α-helix	422-425	4
α-helix	434-446	13
α-helix	454-456	3
α-helix	464-472	9

Chain F: 28 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
α-helix	34	1
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	83-85	3	31
α-helix	88-90	3
β-strand	94-95	2	32
β-strand	101	1	32
β-strand	113-115	3	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	162-169	8
α-helix	170-174	5
β-strand	181-186	6	32
α-helix	190-203	14
β-strand	215-220	6	32
α-helix	226-229	4
α-helix	232-244	13
β-strand	250-256	7	32
α-helix	259-272	14
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	299	1	33
β-strand	303-311	9	32
α-helix	313-315	3
α-helix	320-326	7
β-strand	331-334	4	32
β-strand	335	1	35
α-helix	337-340	4
β-strand	348	1	35
β-strand	355	1	32
α-helix	360-363	4
α-helix	365-382	18
α-helix	385-391	7
α-helix	392-394	3
α-helix	398-414	17
α-helix	419-421	3
α-helix	422-425	4
α-helix	434-445	12
α-helix	454-456	3
α-helix	464-473	10

Chain G: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	3-29	27
α-helix	81-87	7
α-helix	222-269	48

Chain H: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	8-10	3
α-helix	13-39	27

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	272	Bos taurus	P05631 (AlphaFold model)
ATPase inhibitor, mitochondrial	H	protein	84	Bos taurus	P01096 (AlphaFold model)

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

>1OHH_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

>1OHH_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

>1OHH_3 ATP synthase subunit gamma, mitochondrial (chains G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAAL

Sequence of entity 4 (H), FASTA

>1OHH_4 ATPase inhibitor, mitochondrial (chains H)
GSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEI
ERLQKEIERHKQSIKKLKQSEDDD

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	5
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	5

Primary citation

The Structure of Bovine F1-ATPase in Complex with its Regulatory Protein If1. Cabezon, E., Montgomery, M.G., Leslie, A.G.W. et al. Nat Struct Biol (2003) 10:744. DOI 10.1038/NSB966 · 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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