1BMF: Bovine mitochondrial F1-atpase

Bovine mitochondrial F1-atpase. Determined by X-ray diffraction at 2.85 Å resolution. Released 7 Dec 1996.

Method: X-ray diffraction
Resolution: 2.85 Å
Organism: Bos taurus
Chains: 7
Atoms: 23,481
Mol. weight: 353.94 kDa
Ligands: MG, ANP, ADP
Released: 7 Dec 1996

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

Secondary structure: helices and β-sheets

1BMF contains 149 α-helices and 154 β-strands across 7 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, 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	2
β-strand	52-55	4	1
β-strand	60-67	8	1
β-strand	70-75	6	1
α-helix	79-81	3
β-strand	87-90	4	1
β-strand	96-98	3	3
α-helix	101-103	3
β-strand	106-108	3	4
β-strand	114	1	4
β-strand	126-128	3	3
α-helix	132-134	3
β-strand	139	1	5
β-strand	145-146	2	6
α-helix	151-156	6
β-strand	159-160	2	6
β-strand	164	1	4
β-strand	166-169	4	7
α-helix	175-185	11
α-helix	187-190	4
β-strand	199-206	8	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	311	1	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	348-351	4	7
β-strand	352	1	9
α-helix	354-359	6
β-strand	365	1	9
β-strand	371-372	2	7
α-helix	375-378	4
α-helix	381-400	20
α-helix	401-406	6
α-helix	412-427	16
α-helix	435-437	3
α-helix	438-449	12
α-helix	458-474	17
α-helix	477-485	9
α-helix	491-508	18

Chain B: 25 helices, 28 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	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	1	13
α-helix	151-156	6
α-helix	158-159	2
β-strand	160	1	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	240-259	20
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	298-307	10
β-strand	310-311	2	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	354-358	5
β-strand	365	1	16
β-strand	371-372	2	14
α-helix	381-398	18
α-helix	412-428	17
α-helix	435-437	3
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-474	14
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
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	132-134	3
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	166-169	4	22
α-helix	175-185	11
α-helix	187-190	4
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	311	1	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	337-343	7
β-strand	348-352	5	22
α-helix	354-359	6
β-strand	365	1	22
β-strand	371-372	2	22
α-helix	375-378	4
α-helix	381-387	7
α-helix	390-403	14
α-helix	413-427	15
α-helix	435-437	3
α-helix	438-449	12
α-helix	458-474	17
α-helix	477-486	10
α-helix	491-508	18

Chain D: 23 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	1
β-strand	20-25	6	1
α-helix	30-31	2
β-strand	34-38	5	1
β-strand	46-52	7	1
β-strand	57-62	6	1
β-strand	70	1	17
β-strand	74-81	8	1
β-strand	83-86	4	23
α-helix	88-90	3
β-strand	91	1	24
β-strand	94-95	2	24
β-strand	101	1	24
β-strand	112-115	4	23
α-helix	123-125	3
β-strand	126	1	25
β-strand	131-132	2	26
α-helix	138-143	6
β-strand	147-148	2	26
β-strand	151-156	6	24
α-helix	162-169	8
α-helix	170-174	5
β-strand	181-186	6	24
α-helix	190-202	13
β-strand	216-220	5	24
α-helix	226-245	20
β-strand	250-256	7	24
α-helix	259-269	11
α-helix	270-272	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	299	1	25
β-strand	303-311	9	24
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	24
β-strand	335	1	27
α-helix	337-340	4
β-strand	348	1	27
β-strand	354-355	2	24
α-helix	360-363	4
α-helix	365-391	27
α-helix	400-413	14
α-helix	422-425	4
α-helix	434-445	12
α-helix	454-457	4
α-helix	463-473	11

Chain E: 22 helices, 25 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	46-52	7	1
β-strand	57-62	6	1
β-strand	70	1	2
β-strand	74-80	7	1
β-strand	83-86	4	28
α-helix	88-90	3
β-strand	94-95	2	29
β-strand	101	1	29
β-strand	112-115	4	28
β-strand	126	1	30
β-strand	132	1	31
α-helix	133-134	2
α-helix	138-143	6
β-strand	147	1	31
β-strand	151-155	5	29
α-helix	162-177	16
β-strand	181-188	8	29
α-helix	190-202	13
β-strand	215-221	7	29
α-helix	226-245	20
β-strand	250-256	7	29
α-helix	258-271	14
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	298	1	29
β-strand	299	1	30
β-strand	303-309	7	29
α-helix	313-315	3
α-helix	320-326	7
β-strand	331-334	4	29
β-strand	335	1	32
α-helix	337-341	5
β-strand	348	1	32
β-strand	354-355	2	29
α-helix	360-363	4
α-helix	365-391	27
α-helix	400-413	14
α-helix	419-421	3
α-helix	422-425	4
α-helix	434-446	13
α-helix	454-456	3
α-helix	463-472	10

Chain F: 24 helices, 21 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	33
α-helix	88-90	3
β-strand	94-95	2	34
β-strand	101	1	34
β-strand	112-115	4	33
α-helix	119-122	4
α-helix	123-125	3
β-strand	131-133	3	35
α-helix	138-143	6
β-strand	146-148	3	35
β-strand	151-156	6	34
α-helix	162-169	8
α-helix	170-174	5
β-strand	180-186	7	34
α-helix	190-202	13
β-strand	215-220	6	34
α-helix	226-246	21
β-strand	250-256	7	34
α-helix	259-269	11
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	303-311	9	34
α-helix	313-315	3
α-helix	320-323	4
α-helix	326-328	3
β-strand	331-334	4	34
β-strand	335	1	36
α-helix	337-341	5
β-strand	348	1	36
β-strand	354-355	2	34
α-helix	360-391	32
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	463-473	11

Chain G: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	3-42	40
α-helix	81-88	8
α-helix	210-220	11
α-helix	222-270	49

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Bovine mitochondrial F1-atpase	A, B, C	protein	510	Bos taurus	P19483 (AlphaFold model)
Bovine mitochondrial F1-atpase	D, E, F	protein	482	Bos taurus	P00829 (AlphaFold model)
Bovine mitochondrial F1-atpase	G	protein	272	Bos taurus	P05631 (AlphaFold model)

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

>1BMF_1 BOVINE MITOCHONDRIAL F1-ATPASE (chains A, B, C)
QKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
GKIRTDGKISEESDAKLKEIVTNFLAGFEA

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

>1BMF_2 BOVINE MITOCHONDRIAL F1-ATPASE (chains D, E, F)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS

Sequence of entity 3 (G), FASTA

>1BMF_3 BOVINE MITOCHONDRIAL F1-ATPASE (chains G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAAL

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	5
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	4
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1

Primary citation

Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria. Abrahams, J.P., Leslie, A.G., Lutter, R. et al. Nature (1994) 370:621-628. DOI 10.1038/370621a0 · 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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1BMF is part of these collections:

Metabolism and cellular energy

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