1E79: Bovine F1-ATPase inhibited by DCCD

Bovine F1-ATPase inhibited by DCCD (dicyclohexylcarbodiimide). Determined by X-ray diffraction at 2.4 Å resolution. Released 3 Nov 2000.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: BOS TAURUS
Chains: 9
Atoms: 26,318
Mol. weight: 374.93 kDa
Ligands: ATP, MG, ADP, DCW
Released: 3 Nov 2000

Explore 1E79 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1E79 contains 170 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: 28 helices, 25 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	96-99	4	3
α-helix	101-103	3
β-strand	107-109	3	4
β-strand	114	1	4
β-strand	125-128	4	3
α-helix	132-134	3
β-strand	139	1	5
β-strand	145	1	6
α-helix	151-156	6
β-strand	160	1	6
β-strand	164-170	7	4
α-helix	175-185	11
α-helix	187-190	4
α-helix	195-197	3
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	287-289	3
α-helix	291-293	3
α-helix	298-306	9
β-strand	310-311	2	4
β-strand	312	1	5
α-helix	314-316	3
β-strand	320-329	10	4
α-helix	337-345	9
β-strand	348-351	4	4
β-strand	352	1	7
α-helix	354-358	5
β-strand	365	1	7
β-strand	371-372	2	4
α-helix	375-378	4
α-helix	381-400	20
α-helix	401-403	3
α-helix	412-426	15
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-475	15
α-helix	477-482	6
α-helix	483-487	5
α-helix	491-508	18

Chain B: 25 helices, 31 β-strands

Element	Residues	Length	Sheet
β-strand	28-29	2	1
β-strand	33-35	3	1
β-strand	38-41	4	1
β-strand	43	1	1
α-helix	47	1
β-strand	48	1	8
β-strand	51-55	5	1
β-strand	60-67	8	1
β-strand	70-75	6	1
α-helix	79-81	3
β-strand	88-94	7	1
β-strand	96-99	4	9
α-helix	101-103	3
β-strand	107-108	2	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	175-185	11
α-helix	187-190	4
β-strand	200-206	7	10
α-helix	210-221	12
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
β-strand	289	1	14
α-helix	291-293	3
β-strand	295	1	14
α-helix	298-306	9
β-strand	310-311	2	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	349-351	3	13
β-strand	352	1	15
α-helix	354-357	4
β-strand	365	1	15
β-strand	371	1	13
α-helix	373-376	4
α-helix	381-398	18
α-helix	407-409	3
α-helix	414-427	14
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: 29 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	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	17
α-helix	101-103	3
β-strand	107-108	2	18
β-strand	114	1	18
β-strand	126-128	3	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
α-helix	195-197	3
β-strand	200-206	7	18
α-helix	210-223	14
α-helix	226-228	3
β-strand	229-234	6	18
α-helix	240-259	20
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	313	1
α-helix	314-316	3
β-strand	320-325	6	18
β-strand	326-328	3	21
α-helix	337-343	7
β-strand	348-352	5	21
α-helix	354-359	6
β-strand	365	1	21
β-strand	371-372	2	21
α-helix	375-378	4
α-helix	381-387	7
α-helix	390-404	15
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, 23 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	1
β-strand	20-25	6	1
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	83-86	4	22
α-helix	88-90	3
β-strand	91	1	23
β-strand	94-95	2	23
β-strand	101	1	23
β-strand	112-115	4	22
α-helix	119-122	4
α-helix	123-125	3
β-strand	132-133	2	24
α-helix	138-143	6
β-strand	146-147	2	24
β-strand	151-156	6	23
α-helix	162-169	8
α-helix	170-174	5
β-strand	180-186	7	23
α-helix	190-202	13
β-strand	215-220	6	23
α-helix	226-247	22
β-strand	251-256	6	23
α-helix	259-268	10
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
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	25
α-helix	337-340	4
β-strand	348	1	25
β-strand	354-355	2	23
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	454-457	4
α-helix	463-474	12

Chain E: 26 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	1
β-strand	20-24	5	1
α-helix	28-31	4
β-strand	35-38	4	1
β-strand	45-54	10	1
β-strand	57-62	6	1
β-strand	70	1	2
β-strand	74-77	4	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
α-helix	123-125	3
β-strand	126	1	28
β-strand	132	1	29
α-helix	138	1
α-helix	139-143	5
α-helix	145-146	2
β-strand	147	1	29
β-strand	151-155	5	27
α-helix	162-177	16
β-strand	181-188	8	27
α-helix	190-203	14
β-strand	215-221	7	27
α-helix	226-247	22
β-strand	250-256	7	27
α-helix	258-271	14
α-helix	274-276	3
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	320-326	7
β-strand	331-334	4	27
β-strand	335	1	30
α-helix	337-340	4
β-strand	348	1	30
β-strand	355	1	27
α-helix	360-363	4
α-helix	365-389	25
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	464-471	8

Chain F: 26 helices, 23 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	8
β-strand	74-77	4	1
β-strand	83-86	4	31
α-helix	88-90	3
β-strand	91	1	32
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	132-133	2	33
α-helix	138-143	6
β-strand	146-147	2	33
β-strand	151-156	6	32
α-helix	162-169	8
α-helix	170-174	5
β-strand	180-186	7	32
α-helix	190-202	13
β-strand	215-220	6	32
α-helix	226-245	20
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	303-311	9	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	34
α-helix	337-341	5
β-strand	348	1	34
β-strand	354-355	2	32
α-helix	360-363	4
α-helix	365-388	24
α-helix	393-395	3
α-helix	400-413	14
α-helix	419-421	3
α-helix	422-425	4
α-helix	434-446	13
α-helix	454-457	4
α-helix	463-471	9

Chain G: 8 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	3-48	46
β-strand	68-71	4	35
α-helix	81-95	15
β-strand	105-108	4	35
α-helix	110-115	6
α-helix	118-120	3
β-strand	126-129	4	35
α-helix	135-136	2
α-helix	138-149	12
β-strand	158-167	10	35
β-strand	170-178	9	35
α-helix	188-191	4
α-helix	200-271	72

Chain H: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	36
β-strand	26-33	8	36
β-strand	35-37	3	37
β-strand	40	1	38
β-strand	43	1	38
β-strand	46-48	3	37
β-strand	54-57	4	36
β-strand	58	1	38
β-strand	61-66	6	37
β-strand	73-77	5	37
β-strand	80-84	5	36
β-strand	89-94	6	36
β-strand	97-98	2	37
α-helix	100-102	3
α-helix	105-119	15
α-helix	125-142	18

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 alpha chain heart isoform	A, B, C	protein	510	BOS TAURUS	P19483 (AlphaFold model)
ATP synthase beta chain	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

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

>1E79_1 ATP SYNTHASE ALPHA CHAIN HEART ISOFORM (chains A, B, C)
QKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
GKIRTDGKISEESDAKLKEIVTNFLAGFEA

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

>1E79_2 ATP SYNTHASE BETA CHAIN (chains D, E, F)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS

Sequence of entity 3 (G), FASTA

>1E79_3 ATP SYNTHASE GAMMA CHAIN (chains G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAAL

Sequence of entity 4 (H), FASTA

>1E79_4 ATP SYNTHASE DELTA CHAIN (chains H)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE

Sequence of entity 5 (I), FASTA

>1E79_5 ATP SYNTHASE EPSILON CHAIN (chains I)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
MG	Magnesium ion	Mg	5
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	3
DCW	Dicyclohexylurea	C13 H24 N2 O	1

Water and common crystallization additives (GOL, SO4) are not listed.

Primary citation

The Structure of the Central Stalk in Bovine F(1)-ATPase at 2.4 A Resolution. Gibbons, C., Montgomery, M.G., Leslie, A.G.W. et al. Nat Struct Biol (2000) 7:1055. DOI 10.1038/80981 · 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…
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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