7AJJ: Bovine ATP synthase dimer state3:state3
bovine ATP synthase dimer state3:state3. Determined by electron microscopy at 13.1 Å resolution. Released 3 Feb 2021.
- Method
- Electron microscopy
- Resolution
- 13.1 Å
- Organism
- Bos taurus
- Chains
- 58
- Atoms
- 51,424
- Mol. weight
- 1191.11 kDa
- Ligands
- CDL, LHG
- Released
- 3 Feb 2021
Explore 7AJJ in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7AJJ contains 506 α-helices and 382 β-strands across 58 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.
Chains 8 and A8: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-4 | 3 | |
| α-helix | 6-8 | 3 | |
| α-helix | 9-17 | 9 | |
| α-helix | 18-23 | 6 | |
| α-helix | 24-29 | 6 | |
| α-helix | 34-37 | 4 | |
Chains a and Aa: 13 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-9 | 3 | |
| α-helix | 11-12 | 2 | |
| α-helix | 20-25 | 6 | |
| α-helix | 28-30 | 3 | |
| β-strand | 36 | 1 | 97 |
| α-helix | 41-58 | 18 | |
| α-helix | 63-66 | 4 | |
| α-helix | 69-86 | 18 | |
| α-helix | 94-96 | 3 | |
| α-helix | 98-118 | 21 | |
| α-helix | 122-126 | 5 | |
| α-helix | 135-137 | 3 | |
| α-helix | 138-181 | 44 | |
| α-helix | 186-224 | 39 | |
Chains A and AA: 21 helices, 29 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-17 | 9 | |
| β-strand | 26 | 1 | 1 |
| β-strand | 29-33 | 5 | 2 |
| β-strand | 34 | 1 | 3 |
| β-strand | 38-43 | 6 | 2 |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 4 |
| β-strand | 52-55 | 4 | 2 |
| β-strand | 60-66 | 7 | 2 |
| β-strand | 71-75 | 5 | 2 |
| α-helix | 79-81 | 3 | |
| β-strand | 87-90 | 4 | 2 |
| β-strand | 96-98 | 3 | 5 |
| β-strand | 107-109 | 3 | 6 |
| β-strand | 114 | 1 | 6 |
| β-strand | 126-128 | 3 | 5 |
| α-helix | 131-134 | 4 | |
| β-strand | 139 | 1 | 7 |
| β-strand | 145 | 1 | 8 |
| α-helix | 151-155 | 5 | |
| β-strand | 160 | 1 | 8 |
| β-strand | 164 | 1 | 6 |
| β-strand | 166 | 1 | 9 |
| β-strand | 167-169 | 3 | 6 |
| α-helix | 175-185 | 11 | |
| α-helix | 187-191 | 5 | |
| β-strand | 199-206 | 8 | 6 |
| α-helix | 210-222 | 13 | |
| β-strand | 230-234 | 5 | 6 |
| α-helix | 240-259 | 20 | |
| β-strand | 263-269 | 7 | 6 |
| α-helix | 274-285 | 12 | |
| α-helix | 291-293 | 3 | |
| α-helix | 300-306 | 7 | |
| β-strand | 312 | 1 | 7 |
| β-strand | 320-323 | 4 | 6 |
| β-strand | 326-328 | 3 | 6 |
| α-helix | 337-343 | 7 | |
| β-strand | 348-349 | 2 | 9 |
| β-strand | 352 | 1 | 6 |
| α-helix | 354-358 | 5 | |
| β-strand | 365 | 1 | 6 |
| β-strand | 371-372 | 2 | 9 |
| α-helix | 381-399 | 19 | |
| α-helix | 401-403 | 3 | |
| α-helix | 412-428 | 17 | |
| α-helix | 438-449 | 12 | |
| α-helix | 458-473 | 16 | |
| α-helix | 477-485 | 9 | |
| α-helix | 491-506 | 16 | |
Chains Ab and b: 7 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-6 | 5 | |
| β-strand | 12-13 | 2 | 100 |
| β-strand | 17-18 | 2 | 100 |
| α-helix | 19-29 | 11 | |
| α-helix | 32-47 | 16 | |
| α-helix | 55-119 | 65 | |
| α-helix | 120-122 | 3 | |
| α-helix | 123-184 | 62 | |
| α-helix | 190-208 | 19 | |
Chains AB and B: 25 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 9-16 | 8 | |
| α-helix | 19-21 | 3 | |
| β-strand | 28-35 | 8 | 48 |
| β-strand | 38-43 | 6 | 48 |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 49 |
| β-strand | 51 | 1 | 50 |
| β-strand | 52-54 | 3 | 48 |
| β-strand | 60-66 | 7 | 48 |
| β-strand | 71-75 | 5 | 48 |
| α-helix | 79-81 | 3 | |
| β-strand | 87-89 | 3 | 48 |
| β-strand | 94 | 1 | 50 |
| β-strand | 96-99 | 4 | 51 |
| β-strand | 107-109 | 3 | 52 |
| β-strand | 114 | 1 | 52 |
| β-strand | 125-128 | 4 | 51 |
| α-helix | 131-134 | 4 | |
| β-strand | 139 | 1 | 53 |
| β-strand | 145 | 1 | 54 |
| α-helix | 151-156 | 6 | |
| β-strand | 160 | 1 | 54 |
| β-strand | 164 | 1 | 52 |
| β-strand | 167-168 | 2 | 55 |
| α-helix | 175-184 | 10 | |
| α-helix | 185-187 | 3 | |
| β-strand | 199-206 | 8 | 52 |
| α-helix | 210-221 | 12 | |
| β-strand | 229-234 | 6 | 52 |
| α-helix | 240-258 | 19 | |
| β-strand | 263-269 | 7 | 52 |
| α-helix | 271-284 | 14 | |
| α-helix | 291-293 | 3 | |
| α-helix | 300-306 | 7 | |
| β-strand | 312 | 1 | 53 |
| β-strand | 320-323 | 4 | 52 |
| β-strand | 326-327 | 2 | 55 |
| α-helix | 337-343 | 7 | |
| β-strand | 348 | 1 | 56 |
| β-strand | 350-352 | 3 | 55 |
| α-helix | 354-358 | 5 | |
| β-strand | 365-366 | 2 | 55 |
| β-strand | 372 | 1 | 56 |
| α-helix | 375-377 | 3 | |
| α-helix | 381-399 | 19 | |
| α-helix | 400-402 | 3 | |
| α-helix | 412-428 | 17 | |
| α-helix | 438-449 | 12 | |
| α-helix | 452-455 | 4 | |
| α-helix | 458-460 | 3 | |
| α-helix | 461-475 | 15 | |
| α-helix | 477-486 | 10 | |
| α-helix | 491-506 | 16 | |
Chains AC and C: 21 helices, 30 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 28-35 | 8 | 48 |
| β-strand | 38-42 | 5 | 48 |
| α-helix | 47 | 1 | |
| β-strand | 48 | 1 | 62 |
| β-strand | 51-54 | 4 | 48 |
| α-helix | 55 | 1 | |
| β-strand | 60 | 1 | 48 |
| β-strand | 63-66 | 4 | 48 |
| β-strand | 70-74 | 5 | 48 |
| α-helix | 79-81 | 3 | |
| β-strand | 87-94 | 8 | 48 |
| β-strand | 96-98 | 3 | 63 |
| α-helix | 101-103 | 3 | |
| β-strand | 106-109 | 4 | 64 |
| β-strand | 114 | 1 | 64 |
| β-strand | 126-128 | 3 | 63 |
| α-helix | 132-134 | 3 | |
| β-strand | 139 | 1 | 65 |
| β-strand | 145 | 1 | 66 |
| α-helix | 151-155 | 5 | |
| β-strand | 160 | 1 | 66 |
| β-strand | 164 | 1 | 67 |
| β-strand | 167-169 | 3 | 64 |
| α-helix | 175-185 | 11 | |
| α-helix | 187-190 | 4 | |
| β-strand | 199 | 1 | 68 |
| β-strand | 201-206 | 6 | 64 |
| α-helix | 210-221 | 12 | |
| β-strand | 229-234 | 6 | 64 |
| α-helix | 240-259 | 20 | |
| β-strand | 263 | 1 | 68 |
| β-strand | 265-266 | 2 | 67 |
| β-strand | 267-269 | 3 | 64 |
| α-helix | 272-283 | 12 | |
| α-helix | 291-293 | 3 | |
| α-helix | 298-306 | 9 | |
| β-strand | 312 | 1 | 65 |
| β-strand | 322-323 | 2 | 67 |
| β-strand | 326-328 | 3 | 64 |
| α-helix | 337-343 | 7 | |
| β-strand | 348 | 1 | 69 |
| β-strand | 351-352 | 2 | 64 |
| β-strand | 365-366 | 2 | 64 |
| β-strand | 372 | 1 | 69 |
| α-helix | 375-378 | 4 | |
| α-helix | 381-399 | 19 | |
| α-helix | 412-428 | 17 | |
| α-helix | 438-449 | 12 | |
| α-helix | 461-474 | 14 | |
| α-helix | 477-486 | 10 | |
| α-helix | 491-505 | 15 | |
Chains Ad and d: 11 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 12-16 | 5 | |
| α-helix | 24-43 | 20 | |
| α-helix | 53-59 | 7 | |
| α-helix | 65-75 | 11 | |
| α-helix | 89-96 | 8 | |
| α-helix | 97-101 | 5 | |
| α-helix | 104-122 | 19 | |
| α-helix | 125-126 | 2 | |
| α-helix | 127-129 | 3 | |
| β-strand | 131 | 1 | 99 |
| α-helix | 132-138 | 7 | |
| α-helix | 140-142 | 3 | |
Chains AD and D: 23 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-17 | 8 | 48 |
| β-strand | 20-24 | 5 | 48 |
| α-helix | 28-31 | 4 | |
| β-strand | 34-38 | 5 | 48 |
| β-strand | 45-51 | 7 | 48 |
| β-strand | 52 | 1 | 35 |
| β-strand | 57-62 | 6 | 48 |
| β-strand | 70 | 1 | 62 |
| β-strand | 74-81 | 8 | 48 |
| β-strand | 83-86 | 4 | 72 |
| β-strand | 95 | 1 | 73 |
| β-strand | 101 | 1 | 73 |
| β-strand | 112-115 | 4 | 72 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-125 | 3 | |
| β-strand | 126 | 1 | 74 |
| β-strand | 132-133 | 2 | 75 |
| α-helix | 138-143 | 6 | |
| α-helix | 145 | 1 | |
| β-strand | 146-147 | 2 | 75 |
| β-strand | 152-154 | 3 | 76 |
| α-helix | 162-169 | 8 | |
| α-helix | 170-174 | 5 | |
| β-strand | 181-186 | 6 | 76 |
| α-helix | 190-203 | 14 | |
| β-strand | 215-220 | 6 | 76 |
| α-helix | 226-228 | 3 | |
| α-helix | 232-245 | 14 | |
| β-strand | 250-256 | 7 | 76 |
| α-helix | 260-269 | 10 | |
| α-helix | 270-272 | 3 | |
| α-helix | 285-293 | 9 | |
| β-strand | 299 | 1 | 74 |
| β-strand | 303-309 | 7 | 76 |
| α-helix | 313-315 | 3 | |
| α-helix | 320-325 | 6 | |
| α-helix | 326-328 | 3 | |
| β-strand | 331-332 | 2 | 76 |
| β-strand | 335 | 1 | 77 |
| α-helix | 337-340 | 4 | |
| β-strand | 348 | 1 | 77 |
| β-strand | 354 | 1 | 76 |
| α-helix | 360-391 | 32 | |
| α-helix | 398-413 | 16 | |
| α-helix | 420-423 | 4 | |
| α-helix | 434-446 | 13 | |
| α-helix | 454-456 | 3 | |
| α-helix | 463-476 | 14 | |
21 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 protein 8 | 8, A8 | protein | 66 | Bos taurus | P03929 (AlphaFold model) |
| ATP synthase subunit alpha, mitochondrial | A, AA, AB, AC, B, C | protein | 510 | Bos taurus | P19483 (AlphaFold model) |
| ATP synthase subunit beta, mitochondrial | AD, AE, AF, D, E, F | protein | 482 | Bos taurus | P00829 (AlphaFold model) |
| ATP synthase subunit gamma, mitochondrial | AG, G | protein | 273 | Bos taurus | P05631 (AlphaFold model) |
| ATP synthase subunit delta, mitochondrial | AH, H | protein | 146 | Bos taurus | P05630 |
| ATP synthase subunit epsilon, mitochondrial | AI, I | protein | 50 | Bos taurus | P05632 |
| ATPase inhibitor, mitochondrial | AJ, J | protein | 66 | Bos taurus | P01096 |
| ATP synthase F(0) complex subunit C2, mitochondrial | AK, AL, AM, AN, AO, AP, AQ, AR, K, L, M, N, O, P, Q, R | protein | 75 | Bos taurus | P07926 |
| ATP synthase subunit O, mitochondrial | AS, S | protein | 190 | Bos taurus | P13621 |
| ATP synthase subunit a | Aa, a | protein | 226 | Bos taurus | P00847 |
| ATP synthase F(0) complex subunit B1, mitochondrial | Ab, b | protein | 214 | Bos taurus | P13619 |
| ATP synthase subunit d, mitochondrial | Ad, d | protein | 160 | Bos taurus | P13620 |
6 more molecules are not listed.
Sequence of entity 1 (8, A8), FASTA
>7AJJ_1 ATP synthase protein 8 (chains 8, A8)
MPQLDTSTWLTMILSMFLTLFIIFQLKVSKHNFYHNPELTPTKMLKQNTPWETKWTKIYL
PLLLPL
Sequence of entity 2 (A, AA, AB, AC, B, C), FASTA
>7AJJ_2 ATP synthase subunit alpha, mitochondrial (chains A, AA, AB, AC, B, C)
EKTGTAEVSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLK
GMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGP
IGSKARRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAI
DTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAA
PLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKG
IRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSR
GVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVISQHQALL
GKIRTDGKISEESDAKLKEIVTNFLAGFEA
Sequence of entity 3 (AD, AE, AF, D, E, F), FASTA
>7AJJ_3 ATP synthase subunit beta, mitochondrial (chains AD, AE, AF, D, E, F)
AAQASPSPKAGATTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGES
TVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPIKTKQFAAI
HAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKA
HGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTG
LTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERI
TTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSR
IMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQ
PFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEE
HS
Sequence of entity 4 (AG, G), FASTA
>7AJJ_4 ATP synthase subunit gamma, mitochondrial (chains AG, G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAALD
Sequence of entity 5 (AH, H), FASTA
>7AJJ_5 ATP synthase subunit delta, mitochondrial (chains AH, H)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE
Sequence of entity 6 (AI, I), FASTA
>7AJJ_6 ATP synthase subunit epsilon, mitochondrial (chains AI, I)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE
Sequence of entity 7 (AJ, J), FASTA
>7AJJ_7 ATPase inhibitor, mitochondrial (chains AJ, J)
GSESGDNVRSSAGAVRDAGGAFGKREQAEEERYFRARAKEQLAALKKHHENEISHHAKEI
HHHHHH
Sequence of entity 8 (AK, AL, AM, AN, AO, AP, AQ, AR, K, L, M, N, O, P, Q, R), FASTA
>7AJJ_8 ATP synthase F(0) complex subunit C2, mitochondrial (chains AK, AL, AM, AN, AO, AP, AQ, AR, K, L, M, N, O, P, Q, R)
DIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAM
GLFCLMVAFLILFAM
Sequence of entity 9 (AS, S), FASTA
>7AJJ_9 ATP synthase subunit O, mitochondrial (chains AS, S)
FAKLVRPPVQIYGIEGRYATALYSAASKQNKLEQVEKELLRVGQILKEPKMAASLLNPYV
KRSVKVKSLSDMTAKEKFSPLTSNLINLLAENGRLTNTPAVISAFSTMMSVHRGEVPCTV
TTASALDEATLTELKTVLKSFLSKGQVLKLEVKIDPSIMGGMIVRIGEKYVDMSAKTKIQ
KLSRAMREIL
Sequence of entity 10 (Aa, a), FASTA
>7AJJ_10 ATP synthase subunit a (chains Aa, a)
MNENLFTSFITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSI
HNSKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNK
TKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLA
LMSISTTTALITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT
Sequence of entity 11 (Ab, b), FASTA
>7AJJ_11 ATP synthase F(0) complex subunit B1, mitochondrial (chains Ab, b)
PVPPLPEHGGKVRFGLIPEEFFQFLYPKTGVTGPYVLGTGLILYLLSKEIYVITPETFSA
ISTIGFLVYIVKKYGASVGEFADKLNEQKIAQLEEVKQASIKQIQDAIDMEKSQQALVQK
RHYLFDVQRNNIAMALEVTYRERLHRVYREVKNRLDYHISVQNMMRQKEQEHMINWVEKR
VVQSISAQQEKETIAKCIADLKLLSKKAQAQPVM
Sequence of entity 12 (Ad, d), FASTA
>7AJJ_12 ATP synthase subunit d, mitochondrial (chains Ad, d)
AGRKLALKTIDWVAFGEIIPRNQKAVANSLKSWNETLTSRLATLPEKPPAIDWAYYKANV
AKAGLVDDFEKKFNALKVPIPEDKYTAQVDAEEKEDVKSCAEFLTQSKTRIQEYEKELEK
MRNIIPFDQMTIEDLNEVFPETKLDKKKYPYWPHRPIETL
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CDL | Cardiolipin | C81 H156 O17 P2 | 6 |
| LHG | 1,2-dipalmitoyl-phosphatidyl-glycerole | C38 H75 O10 P | 4 |
Primary citation
Interface mobility between monomers in dimeric bovine ATP synthase participates in the ultrastructure of inner mitochondrial membranes. Spikes, T.E., Montgomery, M.G., Walker, J.E. Proc Natl Acad Sci U S A (2021) 118. DOI 10.1073/pnas.2021012118 · PubMed
Other PDB entries of the same protein (UniProt P03929 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6ZQM 3.29 Å, bovine ATP synthase monomer state 2 (combined)
- 9W2R 3.4 Å, Cryo-EM structure of FoF1-ATPase monomer state 1 on the bovine heart submitochondrial…
- 6ZIT 3.49 Å, bovine ATP synthase Stator domain, state 2
- 6ZBB 3.61 Å, bovine ATP synthase Fo domain
- 6ZPO 4.0 Å, bovine ATP synthase monomer state 1 (combined)
- 6ZQN 4.0 Å, bovine ATP synthase monomer state 3 (combined)
- 9W2S 4.0 Å, Cryo-EM structure of FoF1-ATPase monomer state 3 on the bovine heart submitochondrial…
- 9W2T 4.1 Å, Cryo-EM structure of Fo domain of FoF1-ATPase monomer state on the bovine heart…
- 6ZIQ 4.33 Å, bovine ATP synthase stator domain, state 1
- 9VPB 5.0 Å, Cryo-EM structure of the IF1 bound bovine F-ATP synthase planar dimer
- 6ZIU 6.02 Å, bovine ATP synthase stator domain, state 3
- 9VPC 7.2 Å, Cryo-EM structure of the IF1 bound bovine ATP synthase tetramer
Browse structure collections
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