2JIZ: F1-ATPase inhibited by resveratrol

The Structure of F1-ATPase inhibited by resveratrol. Determined by X-ray diffraction at 2.3 Å resolution. Released 21 Aug 2007.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: BOS TAURUS
Chains: 14
Atoms: 50,811
Mol. weight: 709.89 kDa
Ligands: ADP, STL, PO4, AZI
Released: 21 Aug 2007

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

Secondary structure: helices and β-sheets

2JIZ contains 331 α-helices and 314 β-strands across 14 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, 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	2
β-strand	52-55	4	1
β-strand	60-67	8	1
β-strand	70-76	7	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	107-108	2	4
β-strand	114	1	4
β-strand	125-128	4	3
α-helix	132-134	3
β-strand	139	1	5
β-strand	145-146	2	6
α-helix	151-156	6
β-strand	159-160	2	6
β-strand	164	1	4
β-strand	166-170	5	7
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	240-258	19
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	313	1
α-helix	314-316	3
β-strand	320-325	6	4
β-strand	326-329	4	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	381-400	20
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	477-485	9
α-helix	491-508	18

Chain B: 26 helices, 26 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	96-99	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	145-146	2	12
α-helix	151-156	6
β-strand	159-160	2	12
β-strand	164	1	10
β-strand	166-170	5	13
α-helix	175-185	11
α-helix	187-190	4
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	271-284	14
α-helix	287-289	3
α-helix	291-293	3
α-helix	298-306	9
β-strand	311	1	10
β-strand	312	1	11
α-helix	313	1
α-helix	314-316	3
β-strand	320-325	6	10
β-strand	326-329	4	13
α-helix	337-343	7
β-strand	348-352	5	13
α-helix	354-358	5
β-strand	365	1	13
β-strand	371-372	2	13
α-helix	376-378	3
α-helix	381-400	20
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	491-507	17

Chain C: 29 helices, 26 β-strands

Element	Residues	Length	Sheet
α-helix	17-19	3
β-strand	28-35	8	1
β-strand	38-43	6	1
α-helix	47	1
β-strand	48	1	14
β-strand	51-55	5	1
β-strand	60-66	7	1
β-strand	71-75	5	1
β-strand	87-94	8	1
β-strand	96-99	4	15
α-helix	101-103	3
β-strand	107-108	2	16
β-strand	114	1	16
β-strand	125-128	4	15
α-helix	131-134	4
β-strand	139	1	17
β-strand	145	1	18
α-helix	151-156	6
β-strand	160	1	18
β-strand	164	1	16
β-strand	166-169	4	19
α-helix	175-185	11
α-helix	187-190	4
α-helix	195-197	3
β-strand	200-206	7	16
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	16
α-helix	240-258	19
β-strand	263-269	7	16
α-helix	271-284	14
α-helix	287-289	3
α-helix	291-293	3
α-helix	298-306	9
β-strand	311	1	16
β-strand	312	1	17
α-helix	313	1
α-helix	314-316	3
β-strand	320-325	6	16
β-strand	326-328	3	19
α-helix	337-343	7
β-strand	348-352	5	19
α-helix	354-359	6
β-strand	365	1	19
β-strand	371-372	2	19
α-helix	375-378	4
α-helix	381-387	7
α-helix	390-403	14
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	491-508	18

Chain D: 24 helices, 22 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	35-38	4	1
β-strand	46-54	9	1
β-strand	57-62	6	1
β-strand	70	1	14
β-strand	74-77	4	1
β-strand	83-86	4	20
α-helix	88-90	3
β-strand	94-95	2	21
β-strand	101	1	21
β-strand	112-115	4	20
α-helix	119-122	4
α-helix	123-125	3
β-strand	132-133	2	22
α-helix	138-143	6
β-strand	146-147	2	22
β-strand	151-156	6	21
α-helix	162-169	8
α-helix	170-174	5
β-strand	180-186	7	21
α-helix	190-203	14
β-strand	215-220	6	21
α-helix	226-245	20
β-strand	251-256	6	21
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	21
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	21
β-strand	335	1	23
α-helix	337-340	4
β-strand	348	1	23
β-strand	354-355	2	21
α-helix	360-363	4
α-helix	365-391	27
α-helix	400-413	14
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	20-25	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	70	1	2
β-strand	74-77	4	1
β-strand	83-86	4	24
α-helix	88-90	3
β-strand	94-95	2	25
β-strand	101	1	25
β-strand	112-115	4	24
α-helix	119-122	4
α-helix	123-125	3
β-strand	126	1	26
β-strand	132-133	2	27
α-helix	138-143	6
α-helix	145	1
β-strand	146-147	2	27
β-strand	151-155	5	25
α-helix	162-177	16
β-strand	181-188	8	25
α-helix	190-203	14
β-strand	215-221	7	25
α-helix	226-245	20
β-strand	250-256	7	25
α-helix	258-271	14
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	298	1	25
β-strand	299	1	26
β-strand	303-309	7	25
α-helix	313-315	3
α-helix	320-326	7
β-strand	331-334	4	25
β-strand	335	1	28
α-helix	337-341	5
β-strand	348	1	28
β-strand	354-355	2	25
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	428-429	2
α-helix	434-446	13
α-helix	454-457	4
α-helix	463-472	10

Chain F: 27 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	46-54	9	1
β-strand	57-62	6	1
β-strand	70	1	8
β-strand	74-77	4	1
β-strand	83-86	4	29
α-helix	88-90	3
β-strand	91	1	30
β-strand	94-95	2	30
β-strand	101	1	30
β-strand	112-115	4	29
α-helix	119-122	4
α-helix	123-125	3
β-strand	132-133	2	31
α-helix	138-143	6
β-strand	146-147	2	31
β-strand	151-156	6	30
α-helix	162-169	8
α-helix	170-174	5
β-strand	180-186	7	30
α-helix	190-203	14
β-strand	215-220	6	30
α-helix	226-245	20
β-strand	251-256	6	30
α-helix	259-271	13
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	299	1	32
β-strand	302	1	32
β-strand	304-311	8	30
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	30
β-strand	335	1	33
α-helix	337-341	5
β-strand	348	1	33
β-strand	354-355	2	30
α-helix	360-363	4
α-helix	365-383	19
α-helix	385-391	7
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	463-472	10

Chains G and N: 6 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	3-42	40
β-strand	69-71	3	34
α-helix	81-89	9
β-strand	106-108	3	34
α-helix	110-115	6
β-strand	128	1	34
α-helix	138-147	10
β-strand	160-161	2	34
α-helix	163	1
β-strand	164-165	2	35
β-strand	171-172	2	35
α-helix	205-270	66

Chain H: 27 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	28-35	8	36
β-strand	38-43	6	36
α-helix	47	1
β-strand	48	1	37
β-strand	52-55	4	36
β-strand	60-66	7	36
β-strand	71-75	5	36
α-helix	79-81	3
β-strand	87-90	4	36
β-strand	96-99	4	38
α-helix	101-103	3
β-strand	107-108	2	39
β-strand	114	1	39
β-strand	125-128	4	38
α-helix	132-134	3
β-strand	139	1	40
β-strand	145-146	2	41
α-helix	151-156	6
β-strand	159-160	2	41
β-strand	164	1	39
β-strand	166-170	5	42
α-helix	175-185	11
α-helix	187-190	4
α-helix	195-197	3
β-strand	200-206	7	39
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	39
α-helix	240-258	19
β-strand	263-269	7	39
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	39
β-strand	312	1	40
α-helix	314-316	3
β-strand	320-325	6	39
β-strand	326-329	4	42
α-helix	337-345	9
β-strand	348-352	5	42
α-helix	354-359	6
β-strand	365	1	42
β-strand	371-372	2	42
α-helix	375-378	4
α-helix	381-400	20
α-helix	401-403	3
α-helix	412-427	16
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

5 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, H, I, J	protein	510	BOS TAURUS	P19483 (AlphaFold model)
ATP synthase subunit beta	D, E, F, K, L, M	protein	482	BOS TAURUS	P00829 (AlphaFold model)
ATP synthase gamma chain	G, N	protein	272	BOS TAURUS	P05631 (AlphaFold model)

Sequence of entity 1 (A, B, C, H, I, J), FASTA

>2JIZ_1 ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM (chains A, B, C, H, I, J)
EKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
SKIRTDGKISEESDAKLKEIVTNFLAGFEA

Sequence of entity 2 (D, E, F, K, L, M), FASTA

>2JIZ_2 ATP SYNTHASE SUBUNIT BETA (chains D, E, F, K, L, M)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS

Sequence of entity 3 (G, N), FASTA

>2JIZ_3 ATP SYNTHASE GAMMA CHAIN (chains G, N)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAAL

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2
STL	Resveratrol	C14 H12 O3	2
PO4	Phosphate ion	O4 P	2
AZI	Azide ion	N3	2
MG	Magnesium ion	Mg	10
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	8

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

Primary citation

Mechanism of Inhibition of Bovine F1-ATPase by Resveratrol and Related Polyphenols. Gledhill, J.R., Montgomery, M.G., Leslie, A.G.W. et al. Proc Natl Acad Sci U S A (2007) 104:13632. DOI 10.1073/PNAS.0706290104 · 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
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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