7QIN: Actin, alpha skeletal muscle
In situ structure of actomyosin complex in skeletal sarcomere. Determined by electron microscopy at 6.6 Å resolution. Released 16 Feb 2022.
- Method
- Electron microscopy
- Resolution
- 6.6 Å
- Organism
- Mus musculus
- Chains
- 13
- Atoms
- 29,589
- Mol. weight
- 452.37 kDa
- Ligands
- ADP, MG
- Released
- 16 Feb 2022
Explore 7QIN in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
7QIN contains 183 α-helices and 176 β-strands across 13 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 A, B and C: 19 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 1 |
| β-strand | 17-21 | 5 | 1 |
| β-strand | 22 | 1 | 2 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-31 | 3 | 1 |
| β-strand | 35-37 | 3 | 3 |
| β-strand | 42 | 1 | 4 |
| β-strand | 53-54 | 2 | 3 |
| α-helix | 55-61 | 7 | |
| β-strand | 66-68 | 3 | 3 |
| β-strand | 71-72 | 2 | 5 |
| β-strand | 75-76 | 2 | 5 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-94 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 1 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-154 | 5 | 6 |
| β-strand | 160-162 | 3 | 7 |
| β-strand | 163-165 | 3 | 6 |
| β-strand | 166 | 1 | 8 |
| β-strand | 169 | 1 | 8 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 7 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-215 | 13 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 9 |
| β-strand | 247-250 | 4 | 9 |
| α-helix | 253-262 | 10 | |
| α-helix | 274-284 | 11 | |
| α-helix | 290-295 | 6 | |
| β-strand | 298-300 | 3 | 6 |
| α-helix | 301-304 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 330 | 1 | 6 |
| α-helix | 335-348 | 14 | |
| α-helix | 351-355 | 5 | |
| β-strand | 357-358 | 2 | 1 |
| α-helix | 359-364 | 6 | |
| α-helix | 368-373 | 6 | |
Chains D and E: 19 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 27 |
| β-strand | 17-21 | 5 | 27 |
| β-strand | 22 | 1 | 28 |
| β-strand | 24 | 1 | 28 |
| β-strand | 29-31 | 3 | 27 |
| β-strand | 35-37 | 3 | 29 |
| β-strand | 53-54 | 2 | 29 |
| α-helix | 55-61 | 7 | |
| β-strand | 66-68 | 3 | 29 |
| β-strand | 71-72 | 2 | 30 |
| β-strand | 75-76 | 2 | 30 |
| α-helix | 79-88 | 10 | |
| α-helix | 89-94 | 6 | |
| α-helix | 98-100 | 3 | |
| β-strand | 103-107 | 5 | 27 |
| α-helix | 113-125 | 13 | |
| β-strand | 131-136 | 6 | 27 |
| α-helix | 137-145 | 9 | |
| β-strand | 150-154 | 5 | 31 |
| β-strand | 160-162 | 3 | 32 |
| β-strand | 163-165 | 3 | 31 |
| β-strand | 166 | 1 | 13 |
| β-strand | 169 | 1 | 13 |
| α-helix | 172-174 | 3 | |
| β-strand | 176-178 | 3 | 32 |
| α-helix | 182-193 | 12 | |
| α-helix | 203-215 | 13 | |
| α-helix | 223-232 | 10 | |
| β-strand | 238-241 | 4 | 33 |
| β-strand | 247-250 | 4 | 33 |
| α-helix | 253-262 | 10 | |
| α-helix | 274-284 | 11 | |
| α-helix | 290-295 | 6 | |
| β-strand | 298-300 | 3 | 31 |
| α-helix | 301-304 | 4 | |
| α-helix | 309-320 | 12 | |
| β-strand | 330 | 1 | 31 |
| α-helix | 335-348 | 14 | |
| α-helix | 351-355 | 5 | |
| β-strand | 357-358 | 2 | 27 |
| α-helix | 359-364 | 6 | |
| α-helix | 368-373 | 6 | |
Chain F: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-17 | 13 | |
| α-helix | 19-32 | 14 | |
| α-helix | 40-52 | 13 | |
| α-helix | 54-65 | 12 | |
| α-helix | 75-86 | 12 | |
| α-helix | 89-102 | 14 | |
Chain G: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-17 | 13 | |
| α-helix | 19-32 | 14 | |
| α-helix | 40-52 | 13 | |
| α-helix | 54-65 | 12 | |
Chain H: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 81-195 | 115 | |
Chain I: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 80-195 | 116 | |
Chain J: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 79-164 | 86 | |
Chain K: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 80-165 | 86 | |
1 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 |
|---|
| Actin, alpha skeletal muscle | A, B, C, D, E | protein | 371 | Mus musculus | P68134 (AlphaFold model) |
| nebulin (mouse) | F | protein | 105 | Mus musculus | |
| nebulin (mouse) | G | protein | 70 | Mus musculus | |
| tropomyosin, alpha-1 (mouse) | H | protein | 117 | Mus musculus | |
| tropomyosin, alpha-1 (mouse) | I | protein | 118 | Mus musculus | |
| tropomyosin, alpha-1 (mouse) | J, K | protein | 88 | Mus musculus | |
| Myosin-4 | L, M | protein | 848 | Mus musculus | Q5SX39 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>7QIN_1 Actin, alpha skeletal muscle (chains A, B, C, D, E)
TTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGI
LTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMF
ETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRD
LTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPD
GQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTT
MYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDE
AGPSIVHRKCF
Sequence of entity 2 (F), FASTA
>7QIN_2 nebulin (mouse) (chains F)
XXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXX
Sequence of entity 3 (G), FASTA
>7QIN_3 nebulin (mouse) (chains G)
XXXXXXXXXXXXXXXXXXXXXYXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXYXXX
XXXXXXXXXX
Sequence of entity 4 (H), FASTA
>7QIN_4 tropomyosin, alpha-1 (mouse) (chains H)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
Sequence of entity 5 (I), FASTA
>7QIN_5 tropomyosin, alpha-1 (mouse) (chains I)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
Sequence of entity 6 (J, K), FASTA
>7QIN_6 tropomyosin, alpha-1 (mouse) (chains J, K)
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXX
Sequence of entity 7 (L, M), FASTA
>7QIN_7 Myosin-4 (chains L, M)
MSSDAEMAVFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVDAKESYVKATVQSREGGKV
TAKTEGGATVTVKDDQVFSMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSG
LFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGE
SGAGKTVNTKRVIQYFATIAVTGDKKKEEATSGKMQGTLEDQIISANPLLEAFGNAKTVR
NDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPEL
IEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAVDILGFSADEKVAIYKLTGAVM
HYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTV
QQVYNSVGALAKSMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLC
INFTNEKLQQFFNHHMFVLEQEEYKKEGIDWEFIDFGMDLAACIELIEKPMGIFSILEEE
CMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHFSLVHYAGTVDYNIIGWLDKN
KDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKKGGKKKGSSFQTVSALFRENLN
KLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYA
DFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGTLEEM
RDEKLAQLITRTQAVCRGYLMRVEFKKMMERRESIFCIQYNVRAFMNVKHWPWMKLYFKI
KPLLKSAE
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 5 |
| MG | Magnesium ion | Mg | 5 |
Primary citation
Structures from intact myofibrils reveal mechanism of thin filament regulation through nebulin. Wang, Z., Grange, M., Pospich, S. et al. Science (2022) 375:eabn1934-eabn1934. DOI 10.1126/science.abn1934 · PubMed
Other PDB entries of the same protein (UniProt P68134 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4B1U 2.0 Å, Structure of the Phactr1 RPEL domain and RPEL motif directed assemblies with G-actin…
- 6KLL 3.0 Å, F-actin of cardiac thin filament in low-calcium state
- 6KLN 3.4 Å, F-actin of cardiac thin filament in high-calcium state
- 7QIM 4.5 Å, In situ structure of nebulin bound to actin filament in skeletal sarcomere
- 7AQK 9.0 Å, Model of the actin filament Arp2/3 complex branch junction in cells
- 7NEP 10.2 Å, Homology model of the in situ actomyosin complex from the A-band of mouse psoas muscle…
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