6ZBB: Bovine ATP synthase Fo domain
bovine ATP synthase Fo domain. Determined by electron microscopy at 3.61 Å resolution. Released 9 Sept 2020.
- Method
- Electron microscopy
- Resolution
- 3.61 Å
- Organism
- Bos taurus
- Chains
- 17
- Atoms
- 10,490
- Mol. weight
- 185.95 kDa
- Ligands
- LHG, CDL
- Released
- 9 Sept 2020
Explore 6ZBB in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6ZBB contains 80 α-helices and 6 β-strands across 17 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 8: 5 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 | 24-28 | 5 | |
Chain a: 12 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-9 | 3 | |
| α-helix | 11-12 | 2 | |
| α-helix | 20-23 | 4 | |
| α-helix | 26-30 | 5 | |
| β-strand | 36 | 1 | 1 |
| α-helix | 41-57 | 17 | |
| α-helix | 63-66 | 4 | |
| α-helix | 69-86 | 18 | |
| α-helix | 94-96 | 3 | |
| α-helix | 98-126 | 29 | |
| α-helix | 135-137 | 3 | |
| α-helix | 138-181 | 44 | |
| α-helix | 186-224 | 39 | |
Chain b: 5 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-6 | 3 | |
| α-helix | 9-11 | 3 | |
| β-strand | 12-13 | 2 | 2 |
| β-strand | 17-18 | 2 | 2 |
| α-helix | 19-29 | 11 | |
| α-helix | 32-47 | 16 | |
| α-helix | 55-111 | 57 | |
Chain d: 6 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 115-121 | 7 | |
| α-helix | 124-126 | 3 | |
| α-helix | 127-129 | 3 | |
| β-strand | 131 | 1 | 1 |
| α-helix | 132-138 | 7 | |
| α-helix | 140-142 | 3 | |
| α-helix | 146-148 | 3 | |
Chain e: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 8-56 | 49 | |
Chain f: 5 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 15 | 1 | 3 |
| α-helix | 19-25 | 7 | |
| α-helix | 31-44 | 14 | |
| α-helix | 45-49 | 5 | |
| α-helix | 57-73 | 17 | |
| α-helix | 76-79 | 4 | |
Chain g: 5 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 22-36 | 15 | |
| α-helix | 39-41 | 3 | |
| α-helix | 44-61 | 18 | |
| α-helix | 63-66 | 4 | |
| β-strand | 68 | 1 | 3 |
| α-helix | 69-93 | 25 | |
Chain j: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-9 | 7 | |
| α-helix | 14-18 | 5 | |
| α-helix | 20-22 | 3 | |
| α-helix | 24-47 | 24 | |
8 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 | protein | 66 | Bos taurus | P03929 (AlphaFold model) |
| ATP synthase F(0) complex subunit C1, mitochondrial | K, L, M, N, O, P, Q, R | protein | 75 | Bos taurus | P32876 (AlphaFold model) |
| ATP synthase subunit a | a | protein | 226 | Bos taurus | P00847 (AlphaFold model) |
| ATP synthase F(0) complex subunit B1, mitochondrial | b | protein | 214 | Bos taurus | P13619 (AlphaFold model) |
| ATP synthase subunit d, mitochondrial | d | protein | 160 | Bos taurus | P13620 |
| ATP synthase subunit e, mitochondrial | e | protein | 70 | Bos taurus | Q00361 |
| ATP synthase subunit f, mitochondrial | f | protein | 87 | Bos taurus | Q28851 |
| ATP synthase subunit g, mitochondrial | g | protein | 102 | Bos taurus | Q28852 |
| ATP synthase subunit ATP5MPL, mitochondrial | j | protein | 60 | Bos taurus | P14790 |
| ATP synthase membrane subunit DAPIT, mitochondrial | k | protein | 57 | Bos taurus | Q3ZBI7 |
Sequence of entity 1 (8), FASTA
>6ZBB_1 ATP synthase protein 8 (chains 8)
MPQLDTSTWLTMILSMFLTLFIIFQLKVSKHNFYHNPELTPTKMLKQNTPWETKWTKIYL
PLLLPL
Sequence of entity 2 (K, L, M, N, O, P, Q, R), FASTA
>6ZBB_2 ATP synthase F(0) complex subunit C1, mitochondrial (chains K, L, M, N, O, P, Q, R)
DIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAM
GLFCLMVAFLILFAM
Sequence of entity 3 (a), FASTA
>6ZBB_3 ATP synthase subunit a (chains a)
MNENLFTSFITPVILGLPLVTLIVLFPSLLFPTSNRLVSNRFVTLQQWMLQLVSKQMMSI
HNSKGQTWTLMLMSLILFIGSTNLLGLLPHSFTPTTQLSMNLGMAIPLWAGAVITGFRNK
TKASLAHFLPQGTPTPLIPMLVIIETISLFIQPMALAVRLTANITAGHLLIHLIGGATLA
LMSISTTTALITFTILILLTILEFAVAMIQAYVFTLLVSLYLHDNT
Sequence of entity 4 (b), FASTA
>6ZBB_4 ATP synthase F(0) complex subunit B1, mitochondrial (chains b)
PVPPLPEHGGKVRFGLIPEEFFQFLYPKTGVTGPYVLGTGLILYLLSKEIYVITPETFSA
ISTIGFLVYIVKKYGASVGEFADKLNEQKIAQLEEVKQASIKQIQDAIDMEKSQQALVQK
RHYLFDVQRNNIAMALEVTYRERLHRVYREVKNRLDYHISVQNMMRQKEQEHMINWVEKR
VVQSISAQQEKETIAKCIADLKLLSKKAQAQPVM
Sequence of entity 5 (d), FASTA
>6ZBB_5 ATP synthase subunit d, mitochondrial (chains d)
AGRKLALKTIDWVAFGEIIPRNQKAVANSLKSWNETLTSRLATLPEKPPAIDWAYYKANV
AKAGLVDDFEKKFNALKVPIPEDKYTAQVDAEEKEDVKSCAEFLTQSKTRIQEYEKELEK
MRNIIPFDQMTIEDLNEVFPETKLDKKKYPYWPHRPIETL
Sequence of entity 6 (e), FASTA
>6ZBB_6 ATP synthase subunit e, mitochondrial (chains e)
VPPVQVSPLIKLGRYSALFLGMAYGAKRYNYLKPRAEEERRLAAEEKKKRDEQKRIEREL
AEAQEDTILK
Sequence of entity 7 (f), FASTA
>6ZBB_7 ATP synthase subunit f, mitochondrial (chains f)
ASVVPLKEKKLLEVKLGELPSWILMRDFTPSGIAGAFQRGYYRYYNKYVNVKKGSIAGLS
MVLAAYVFLNYCRSYKELKHERLRKYH
Sequence of entity 8 (g), FASTA
>6ZBB_8 ATP synthase subunit g, mitochondrial (chains g)
AEFVRNLAEKAPALVNAAVTYSKPRLATFWYYAKVELVPPTPAEIPTAIQSLKKIINSAK
TGSFKQLTVKEALLNGLVATEVWMWFYVGEIIGKRGIIGYDV
Sequence of entity 9 (j), FASTA
>6ZBB_9 ATP synthase subunit ATP5MPL, mitochondrial (chains j)
MLQSLIKKVWIPMKPYYTQAYQEIWVGTGLMAYIVYKIRSADKRSKALKASSAAPAHGHH
Sequence of entity 10 (k), FASTA
>6ZBB_10 ATP synthase membrane subunit DAPIT, mitochondrial (chains k)
AGPEADAQFHFTGIKKYFNSYTLTGRMNCVLATYGSIALIVLYFKLRSKKTPAVKAT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| LHG | 1,2-dipalmitoyl-phosphatidyl-glycerole | C38 H75 O10 P | 2 |
| CDL | Cardiolipin | C81 H156 O17 P2 | 3 |
Primary citation
Structure of the dimeric ATP synthase from bovine mitochondria. Spikes, T.E., Montgomery, M.G., Walker, J.E. Proc Natl Acad Sci U S A (2020) 117:23519-23526. DOI 10.1073/pnas.2013998117 · 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
- 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
- 7AJF 8.45 Å, bovine ATP synthase dimer state2:state2
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