6ZG7: Bovine ATP synthase rotor domain, state 1
bovine ATP synthase rotor domain, state 1. Determined by electron microscopy at 3.49 Å resolution. Released 9 Sept 2020.
- Method
- Electron microscopy
- Resolution
- 3.49 Å
- Organism
- Bos taurus
- Chains
- 11
- Atoms
- 7,735
- Mol. weight
- 112.26 kDa
- Released
- 9 Sept 2020
Explore 6ZG7 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6ZG7 contains 55 α-helices and 21 β-strands across 11 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 G: 7 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-47 | 45 | |
| α-helix | 51-54 | 4 | |
| β-strand | 66-71 | 6 | 1 |
| α-helix | 80-97 | 18 | |
| β-strand | 103-108 | 6 | 1 |
| α-helix | 110-120 | 11 | |
| β-strand | 124-129 | 6 | 1 |
| α-helix | 138-150 | 13 | |
| β-strand | 157-164 | 8 | 1 |
| β-strand | 172-179 | 8 | 1 |
| α-helix | 181-185 | 5 | |
| β-strand | 194 | 1 | 2 |
| α-helix | 200-271 | 72 | |
Chain H: 4 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 17-21 | 5 | 2 |
| β-strand | 26-31 | 6 | 2 |
| β-strand | 33-38 | 6 | 3 |
| β-strand | 40 | 1 | 4 |
| β-strand | 45-47 | 3 | 3 |
| α-helix | 51-53 | 3 | |
| β-strand | 54 | 1 | 2 |
| β-strand | 58 | 1 | 4 |
| β-strand | 61-67 | 7 | 3 |
| β-strand | 73-77 | 5 | 3 |
| β-strand | 80-84 | 5 | 2 |
| β-strand | 89-94 | 6 | 2 |
| β-strand | 97-99 | 3 | 3 |
| α-helix | 100-102 | 3 | |
| β-strand | 103 | 1 | 5 |
| α-helix | 105-119 | 15 | |
| α-helix | 125-145 | 21 | |
Chain I: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-6 | 4 | |
| α-helix | 11-24 | 14 | |
| β-strand | 26 | 1 | 5 |
| α-helix | 28-35 | 8 | |
| β-strand | 43-45 | 3 | 1 |
| α-helix | 46 | 1 | |
Chain K: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-13 | 12 | |
| α-helix | 15-17 | 3 | |
| α-helix | 18-38 | 21 | |
| α-helix | 40-42 | 3 | |
| α-helix | 45-72 | 28 | |
Chain L: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-14 | 13 | |
| α-helix | 16-18 | 3 | |
| α-helix | 19-38 | 20 | |
| α-helix | 44-72 | 29 | |
Chain M: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-14 | 12 | |
| α-helix | 15-17 | 3 | |
| α-helix | 18-38 | 21 | |
| α-helix | 40-42 | 3 | |
| α-helix | 43-69 | 27 | |
| α-helix | 70-74 | 5 | |
Chain N: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-14 | 13 | |
| α-helix | 18-38 | 21 | |
| α-helix | 40-42 | 3 | |
| α-helix | 43-73 | 31 | |
Chain O: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-14 | 12 | |
| α-helix | 15-17 | 3 | |
| α-helix | 18-38 | 21 | |
| α-helix | 40-42 | 3 | |
| α-helix | 43-73 | 31 | |
3 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 gamma, mitochondrial | G | protein | 273 | Bos taurus | P05631 (AlphaFold model) |
| ATP synthase subunit delta, mitochondrial | H | protein | 146 | Bos taurus | P05630 (AlphaFold model) |
| ATP synthase subunit epsilon, mitochondrial | I | protein | 50 | Bos taurus | P05632 (AlphaFold model) |
| ATP synthase F(0) complex subunit C2, mitochondrial | K, L, M, N, O, P, Q, R | protein | 75 | Bos taurus | P07926 (AlphaFold model) |
Sequence of entity 1 (G), FASTA
>6ZG7_1 ATP synthase subunit gamma, mitochondrial (chains G)
ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKPARVYGVGSLALYEKADIKTP
EDKKKHLIIGVSSDRGLCGAIHSSVAKQMKSEAANLAAAGKEVKIIGVGDKIRSILHRTH
SDQFLVTFKEVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVISYKTEEKPIFS
LDTISSAESMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS
EMIDKLTLTFNRTRQAVITKELIEIISGAAALD
Sequence of entity 2 (H), FASTA
>6ZG7_2 ATP synthase subunit delta, mitochondrial (chains H)
AEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRP
GLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELL
GAADEATRAEIQIRIEANEALVKALE
Sequence of entity 3 (I), FASTA
>6ZG7_3 ATP synthase subunit epsilon, mitochondrial (chains I)
VAYWRQAGLSYIRYSQICAKAVRDALKTEFKANAMKTSGSTIKIVKVKKE
Sequence of entity 4 (K, L, M, N, O, P, Q, R), FASTA
>6ZG7_4 ATP synthase F(0) complex subunit C2, mitochondrial (chains K, L, M, N, O, P, Q, R)
DIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAM
GLFCLMVAFLILFAM
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 P05631 (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
Browse structure collections
About this viewer
MolViewer shows 6ZG7 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.