2WSS: Membrane extrinsic region of bovine ATP synthase

The structure of the membrane extrinsic region of bovine ATP synthase. Determined by X-ray diffraction at 3.2 Å resolution. Released 17 Nov 2009.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: BOS TAURUS
Chains: 25
Atoms: 54,949
Mol. weight: 851.83 kDa
Ligands: ADP, MG, ANP
Released: 17 Nov 2009

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

Secondary structure: helices and β-sheets

2WSS contains 339 α-helices and 363 β-strands across 23 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, 28 β-strands

Element	Residues	Length	Sheet
α-helix	10-17	8
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	60-66	7	1
β-strand	71-76	6	1
β-strand	87-93	7	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	1	4
β-strand	166-169	4	7
α-helix	175-190	16
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	291-293	3
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
β-strand	330	1	8
β-strand	333	1	8
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	381-399	19
α-helix	401-404	4
α-helix	412-427	16
α-helix	435-437	3
α-helix	438-449	12
α-helix	458-474	17
α-helix	478-486	9
α-helix	491-508	18

Chain B: 25 helices, 28 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	9
β-strand	51	1	10
β-strand	54-55	2	1
β-strand	60-66	7	1
β-strand	71-75	5	1
β-strand	87-89	3	1
α-helix	93	1
β-strand	94	1	10
β-strand	96-99	4	11
α-helix	101-103	3
β-strand	107-108	2	12
β-strand	114	1	12
β-strand	125-128	4	11
α-helix	131-133	3
β-strand	139	1	13
β-strand	145-146	2	14
α-helix	151-156	6
β-strand	159-160	2	14
β-strand	164	1	12
β-strand	166-170	5	15
α-helix	175-185	11
α-helix	187-190	4
β-strand	200-206	7	12
α-helix	210-222	13
α-helix	226-228	3
β-strand	229-234	6	12
α-helix	240-259	20
β-strand	263-269	7	12
α-helix	271-284	14
α-helix	287-289	3
α-helix	291-293	3
α-helix	300-306	7
β-strand	311	1	12
β-strand	312	1	13
α-helix	314-316	3
β-strand	320-325	6	12
β-strand	326-329	4	15
α-helix	337-343	7
β-strand	348-352	5	15
α-helix	354-359	6
β-strand	365	1	15
β-strand	371-372	2	15
α-helix	374-378	5
α-helix	381-398	18
α-helix	412-428	17
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-474	14
α-helix	477-485	9
α-helix	491-504	14

Chain C: 24 helices, 32 β-strands

Element	Residues	Length	Sheet
β-strand	33-35	3	1
β-strand	38-40	3	1
α-helix	47	1
β-strand	48	1	16
β-strand	51-55	5	17
β-strand	60	1	17
β-strand	63-67	5	1
β-strand	70-74	5	1
β-strand	88-94	7	17
α-helix	95	1
β-strand	96-98	3	18
α-helix	101-103	3
β-strand	108	1	19
β-strand	114	1	19
β-strand	126-128	3	18
α-helix	131-134	4
β-strand	139	1	20
β-strand	145	1	21
α-helix	151-156	6
β-strand	160	1	21
β-strand	164	1	22
β-strand	166-169	4	23
α-helix	176-183	8
α-helix	187-190	4
β-strand	200-206	7	22
α-helix	210-223	14
α-helix	226-228	3
β-strand	229	1	22
β-strand	232	1	19
β-strand	233-234	2	22
α-helix	240-259	20
β-strand	263-269	7	22
α-helix	271-284	14
α-helix	291-293	3
α-helix	298-307	10
β-strand	311	1	22
β-strand	312	1	20
α-helix	314-316	3
β-strand	320-325	6	22
β-strand	326-328	3	23
β-strand	330	1	24
β-strand	333	1	24
α-helix	337-345	9
β-strand	348-351	4	23
α-helix	354-359	6
β-strand	371-372	2	23
α-helix	375-378	4
β-strand	381	1	25
α-helix	416-428	13
α-helix	438-449	12
α-helix	458-460	3
α-helix	461-468	8
α-helix	471-474	4
α-helix	477-486	10
β-strand	488	1	25
α-helix	491-500	10

Chain D: 23 helices, 23 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	35-39	5	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	83-84	2	26
α-helix	88-90	3
β-strand	94	1	27
β-strand	114-115	2	26
α-helix	123-125	3
β-strand	126	1	28
β-strand	132-133	2	29
α-helix	138-143	6
β-strand	146-147	2	29
β-strand	151-156	6	27
α-helix	162-172	11
β-strand	181-186	6	27
α-helix	190-202	13
β-strand	215-220	6	27
α-helix	226-245	20
β-strand	250-256	7	27
α-helix	259-269	11
α-helix	270-272	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	299	1	28
β-strand	303-311	9	27
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	27
β-strand	335	1	30
α-helix	337-340	4
β-strand	348	1	30
β-strand	354-355	2	27
α-helix	360-383	24
α-helix	385-388	4
α-helix	393-395	3
α-helix	398-413	16
α-helix	419-421	3
α-helix	434-446	13
α-helix	454-456	3
α-helix	464-472	9

Chain E: 24 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	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	83-85	3	31
α-helix	88-90	3
β-strand	91	1	32
β-strand	94-95	2	32
β-strand	101	1	32
β-strand	113-115	3	31
α-helix	123-125	3
β-strand	126	1	32
β-strand	132	1	33
α-helix	133-134	2
α-helix	138-143	6
α-helix	145-146	2
β-strand	147	1	33
β-strand	151-155	5	32
α-helix	162-175	14
β-strand	181-186	6	32
α-helix	190-203	14
β-strand	215-220	6	32
α-helix	226-245	20
β-strand	250-256	7	32
α-helix	258-271	14
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-293	9
β-strand	298-299	2	32
β-strand	302-309	8	32
α-helix	313-315	3
α-helix	320-327	8
β-strand	331-334	4	32
β-strand	335	1	34
α-helix	337-341	5
β-strand	348	1	34
β-strand	355	1	32
α-helix	366-387	22
α-helix	400-413	14
α-helix	419-421	3
α-helix	422-425	4
α-helix	428-430	3
α-helix	434-445	12
α-helix	463-465	3
α-helix	467-470	4

Chain F: 23 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	10-17	8	1
β-strand	20-25	6	1
α-helix	34	1
β-strand	35-39	5	1
β-strand	46-54	9	1
β-strand	57-61	5	1
β-strand	70	1	9
β-strand	72-77	6	1
β-strand	83-85	3	35
α-helix	88-90	3
β-strand	94-95	2	36
β-strand	101	1	36
β-strand	113-115	3	35
α-helix	123-125	3
β-strand	126	1	37
β-strand	132-133	2	38
α-helix	138-143	6
β-strand	146-147	2	38
β-strand	151-156	6	36
α-helix	162-172	11
β-strand	181-186	6	36
α-helix	190-202	13
β-strand	215-220	6	36
α-helix	226-245	20
β-strand	250-256	7	36
α-helix	259-272	14
α-helix	274-276	3
α-helix	278-280	3
α-helix	285-295	11
β-strand	299	1	37
β-strand	303-311	9	36
α-helix	313-315	3
α-helix	320-325	6
α-helix	326-328	3
β-strand	331-334	4	36
β-strand	335	1	39
α-helix	337-340	4
β-strand	348	1	39
β-strand	354-355	2	36
α-helix	360-363	4
α-helix	367-384	18
α-helix	387-390	4
α-helix	393-395	3
α-helix	398-413	16
α-helix	434-445	12
α-helix	455-457	3
α-helix	463-473	11

Chains G and P: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	3-36	34
α-helix	38-50	13
α-helix	80-83	4
β-strand	105-106	2	40
α-helix	110-114	5
β-strand	124-126	3	40
β-strand	127	1	41
β-strand	131	1	42
β-strand	134	1	42
α-helix	138-149	12
β-strand	160-163	4	43
β-strand	167	1	44
β-strand	170	1	44
β-strand	173-176	4	43
α-helix	182-185	4
α-helix	205-220	16
α-helix	225-270	46

Chains H and Q: 4 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	16-21	6	45
β-strand	26-33	8	45
β-strand	35-37	3	46
β-strand	39	1	47
β-strand	44	1	47
α-helix	51-53	3
β-strand	54-56	3	45
β-strand	61-66	6	46
β-strand	74-77	4	46
β-strand	81-85	5	45
β-strand	89-93	5	45
α-helix	105-108	4
α-helix	113-120	8
α-helix	126-141	16

12 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, mitochondrial	A, B, C, J, K, L	protein	510	BOS TAURUS	P19483 (AlphaFold model)
ATP synthase subunit beta, mitochondrial	D, E, F, M, N, O	protein	482	BOS TAURUS	P00829 (AlphaFold model)
ATP synthase subunit gamma, mitochondrial	G, P	protein	272	BOS TAURUS	P05631 (AlphaFold model)
ATP synthase subunit delta, mitochondrial	H, Q	protein	146	BOS TAURUS	P05630 (AlphaFold model)
ATP synthase subunit epsilon, mitochondrial	I, R	protein	50	BOS TAURUS	P05632
ATP synthase subunit O, mitochondrial	S, W	protein	190	BOS TAURUS	P13621
ATP synthase subunit B, mitochondrial	T, X	protein	116	BOS TAURUS	P13619
ATP synthase subunit D, mitochondrial	U	protein	118	BOS TAURUS	P13620
ATP synthase-coupling factor 6, mitochondrial	V, Z	protein	76	BOS TAURUS	P02721

Sequence of entity 1 (A, B, C, J, K, L), FASTA

>2WSS_1 ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL (chains A, B, C, J, K, L)
QKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
GKIRTDGKISEESDAKLKEIVTNFLAGFEA

Sequence of entity 2 (D, E, F, M, N, O), FASTA

>2WSS_2 ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL (chains D, E, F, M, N, O)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS

Sequence of entity 3 (G, P), FASTA

>2WSS_3 ATP SYNTHASE SUBUNIT GAMMA, MITOCHONDRIAL (chains G, P)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAAL

Sequence of entity 4 (H, Q), FASTA

>2WSS_4 ATP SYNTHASE SUBUNIT DELTA, MITOCHONDRIAL (chains H, Q)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE

Sequence of entity 5 (I, R), FASTA

>2WSS_5 ATP SYNTHASE SUBUNIT EPSILON, MITOCHONDRIAL (chains I, R)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE

Sequence of entity 6 (S, W), FASTA

>2WSS_6 ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL (chains S, W)
FAKLVRPPVQIYGIEGRYATALYSAASKQNKLEQVEKELLRVGQILKEPKMAASLLNPYV
KRSVKVKSLSDMTAKEKFSPLTSNLINLLAENGRLTNTPAVISAFSTMMSVHRGEVPCTV
TTASALDETTLTELKTVLKSFLSKGQVLKLEVKIDPSIMGGMIVRIGEKYVDMSAKTKIQ
KLSRAMREIL

Sequence of entity 7 (T, X), FASTA

>2WSS_7 ATP SYNTHASE SUBUNIT B, MITOCHONDRIAL (chains T, X)
ASIKQIQDAIDMEKSQQALVQKRHYLFDVQRNNIAMALEVTYRERLHRVYREVKNRLDYH
ISVQNMMRQKEQEHMINWVEKRVVQSISAQQEKETIAKCIADLKLLSKKAQAQPVM

Sequence of entity 8 (U), FASTA

>2WSS_8 ATP SYNTHASE SUBUNIT D, MITOCHONDRIAL (chains U)
AGRKLALKTIDWVAFGEIIPRNQKAVANSLKSWNETLTSRLATLPEKPPAIDWAYYKANV
AKAGLVDDFEKKFNALKVPIPEDKYTAQVDAEEKEDVKSCAEFLTQSKTRIQEYEKEL

Sequence of entity 9 (V, Z), FASTA

>2WSS_9 ATP SYNTHASE-COUPLING FACTOR 6, MITOCHONDRIAL (chains V, Z)
NKELDPVQKLFVDKIREYRTKRQTSGGPVDAGPEYQQDLDRELFKLKQMYGKADMNTFPN
FTFEDPKFEVVEKPQS

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	2
MG	Magnesium ion	Mg	10
ANP	Phosphoaminophosphonic acid-adenylate ester	C10 H17 N6 O12 P3	8

Primary citation

The Structure of the Membrane Extrinsic Region of Bovine ATP Synthase. Rees, D.M., Leslie, A.G.W., Walker, J.E. Proc Natl Acad Sci U S A (2009) 106:21597. DOI 10.1073/PNAS.0910365106 · 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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