Cryo-EM structure of the divergent actomyosin complex from Plasmodium falciparum Myosin A in the Rigor state. Determined by electron microscopy at 3.77 Å resolution. Released 28 Apr 2021.
Explore 7ALN in 3D Show helices and sheets RCSB PDB PDBe
7ALN contains 140 α-helices and 125 β-strands across 6 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-13 | 5 | 1 |
| β-strand | 18-22 | 5 | 1 |
| β-strand | 30-32 | 3 | 1 |
| β-strand | 36-39 | 4 | 2 |
| β-strand | 43 | 1 | 3 |
| β-strand | 54-55 | 2 | 2 |
| α-helix | 57-61 | 5 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-69 | 4 | 2 |
| β-strand | 72-73 | 2 | 4 |
| β-strand | 76-77 | 2 | 4 |
| α-helix | 80-88 | 9 | |
| α-helix | 89-95 | 7 | |
| β-strand | 104-108 | 5 | 1 |
| α-helix | 114-122 | 9 | |
| α-helix | 123-127 | 5 | |
| β-strand | 132 | 1 | 5 |
| β-strand | 133-137 | 5 | 1 |
| α-helix | 138-145 | 8 | |
| β-strand | 150-154 | 5 | 6 |
| β-strand | 163-167 | 5 | 6 |
| β-strand | 170-171 | 2 | 6 |
| α-helix | 183-197 | 15 | |
| α-helix | 204-217 | 14 | |
| α-helix | 224-230 | 7 | |
| β-strand | 239-242 | 4 | 7 |
| β-strand | 248-251 | 4 | 7 |
| α-helix | 253-255 | 3 | |
| α-helix | 260-262 | 3 | |
| α-helix | 265-267 | 3 | |
| α-helix | 275-284 | 10 | |
| α-helix | 291-295 | 5 | |
| β-strand | 298-300 | 3 | 6 |
| α-helix | 303-305 | 3 | |
| α-helix | 310-321 | 12 | |
| β-strand | 330-331 | 2 | 6 |
| α-helix | 339-348 | 10 | |
| α-helix | 353-355 | 3 | |
| β-strand | 359 | 1 | 5 |
| α-helix | 360-366 | 7 | |
| α-helix | 367-372 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-13 | 5 | 8 |
| β-strand | 18-22 | 5 | 8 |
| β-strand | 30-32 | 3 | 8 |
| β-strand | 36-39 | 4 | 9 |
| β-strand | 54-55 | 2 | 9 |
| α-helix | 57-61 | 5 | |
| α-helix | 63-65 | 3 | |
| β-strand | 66-69 | 4 | 9 |
| β-strand | 72-73 | 2 | 10 |
| β-strand | 76-77 | 2 | 10 |
| α-helix | 80-88 | 9 | |
| α-helix | 89-95 | 7 | |
| β-strand | 104-108 | 5 | 8 |
| α-helix | 114-122 | 9 | |
| α-helix | 123-127 | 5 | |
| β-strand | 132 | 1 | 11 |
| β-strand | 133-137 | 5 | 8 |
| α-helix | 138-145 | 8 | |
| β-strand | 150-154 | 5 | 3 |
| β-strand | 163-167 | 5 | 3 |
| β-strand | 170-171 | 2 | 3 |
| α-helix | 183-197 | 15 | |
| α-helix | 204-217 | 14 | |
| α-helix | 224-230 | 7 | |
| β-strand | 239-242 | 4 | 12 |
| β-strand | 248-251 | 4 | 12 |
| α-helix | 253-255 | 3 | |
| α-helix | 260-262 | 3 | |
| α-helix | 265-267 | 3 | |
| α-helix | 275-284 | 10 | |
| α-helix | 291-295 | 5 | |
| β-strand | 298-300 | 3 | 3 |
| α-helix | 303-305 | 3 | |
| α-helix | 310-321 | 12 | |
| β-strand | 330-331 | 2 | 3 |
| α-helix | 339-348 | 10 | |
| α-helix | 353-355 | 3 | |
| β-strand | 359 | 1 | 11 |
| α-helix | 360-366 | 7 | |
| α-helix | 367-372 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-14 | 10 | |
| α-helix | 20-22 | 3 | |
| β-strand | 24 | 1 | 31 |
| β-strand | 31 | 1 | 31 |
| β-strand | 35-38 | 4 | 32 |
| α-helix | 42-46 | 5 | |
| β-strand | 53-57 | 5 | 32 |
| α-helix | 58 | 1 | |
| β-strand | 66-72 | 7 | 32 |
| β-strand | 80-82 | 3 | 32 |
| β-strand | 87-88 | 2 | 32 |
| α-helix | 102-104 | 3 | |
| α-helix | 110-122 | 13 | |
| β-strand | 127-128 | 2 | 33 |
| β-strand | 133-137 | 5 | 33 |
| α-helix | 148-156 | 9 | |
| α-helix | 164 | 1 | |
| α-helix | 167-180 | 14 | |
| β-strand | 185-191 | 7 | 33 |
| α-helix | 197-209 | 13 | |
| α-helix | 220-226 | 7 | |
| α-helix | 228-235 | 8 | |
| β-strand | 236-239 | 4 | 34 |
| β-strand | 242-246 | 5 | 34 |
| β-strand | 249-256 | 8 | 33 |
| α-helix | 257 | 1 | |
| β-strand | 262-270 | 9 | 33 |
| β-strand | 287 | 1 | 34 |
| α-helix | 289-296 | 8 | |
| α-helix | 299-305 | 7 | |
| α-helix | 331-340 | 10 | |
| α-helix | 346-362 | 17 | |
| β-strand | 367-369 | 3 | 35 |
| β-strand | 379-381 | 3 | 35 |
| α-helix | 386-395 | 10 | |
| α-helix | 400-408 | 9 | |
| β-strand | 409-413 | 5 | 36 |
| β-strand | 418-422 | 5 | 36 |
| α-helix | 425-455 | 31 | |
| β-strand | 465-470 | 6 | 33 |
| α-helix | 481-511 | 31 | |
| α-helix | 516-518 | 3 | |
| α-helix | 525-532 | 8 | |
| α-helix | 538-547 | 10 | |
| α-helix | 554-563 | 10 | |
| β-strand | 570-572 | 3 | 37 |
| β-strand | 580-585 | 6 | 37 |
| β-strand | 588-593 | 6 | 37 |
| α-helix | 597-601 | 5 | |
| α-helix | 607-614 | 8 | |
| α-helix | 619-624 | 6 | |
| α-helix | 641-657 | 17 | |
| β-strand | 660-667 | 8 | 33 |
| α-helix | 680-689 | 10 | |
| α-helix | 692-699 | 8 | |
| β-strand | 705-708 | 4 | 38 |
| α-helix | 709-715 | 7 | |
| α-helix | 721-724 | 4 | |
| α-helix | 731-741 | 11 | |
| β-strand | 749-751 | 3 | 38 |
| β-strand | 755-758 | 4 | 38 |
| α-helix | 760-766 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Actin-1 | A, B, C, D, E | protein | 376 | Plasmodium falciparum (isolate 3D7) | Q8I4X0 (AlphaFold model) |
| Myosin-A | F | protein | 818 | Plasmodium falciparum (isolate 3D7) | Q8IDR3 (AlphaFold model) |
>7ALN_1 Actin-1 (chains A, B, C, D, E) MGEEDVQALVVDNGSGNVKAGVAGDDAPRSVFPSIVGRPKNPGIMVGMEEKDAFVGDEAQ TKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRAAPEEHPVLLTEAPLNPKGNRERM TQIMFESFNVPAMYVAIQAVLSLYSSGRTTGIVLDSGDGVSHTVPIYEGYALPHAIMRLD LAGRDLTEYLMKILHERGYGFSTSAEKEIVRDIKEKLCYIALNFDEEMKTSEQSSDIEKS YELPDGNIITVGNERFRCPEALFQPSFLGKEAAGIHTTTFNSIKKCDVDIRKDLYGNIVL SGGTTMYEGIGERLTRDITTLAPSTMKIKVVAPPERKYSVWIGGSILSSLSTFQQMWITK EEYDESGPSIVHRKCF
>7ALN_2 Myosin-A (chains F) MAVTNEEIKTASKIVRRVSNVEAFDKSGSVFKGYQIWTDISPTIENDPNIMFVKCVVQQG SKKEKLTVVQIDPPGTGTPYDIDPTHAWNCNSQVDPMSFGDIGLLNHTNIPCVLDFLKHR YLKNQIYTTAVPLIVAINPYKDLGNTTNEWIRRYRDTADHTKLPPHVFTCAREALSNLHG VNKSQTIIVSGESGAGKTEATKQIMRYFASSKSGNMDLRIQTAIMAANPVLEAFGNAKTI RNNNSSRFGRFMQLVISHEGGIRYGSVVAFLLEKSRIITQDDNERSYHIFYQFLKGANST MKSKFGLKGVTEYKLLNPNSTEVSGVDDVKDFEEVIESLKNMELSESDIEVIFSIVAGIL TLGNVRLIEKQEAGLSDAAAIMDEDMGVFNKACELMYLDPELIKREILIKVTVAGGDKIE GRWNKNDAEVLKSSLCKAMYEKLFLWIIRHLNSRIEPEGGFKTFMGMLDIFGFEVFKNNS LEQLFINITNEMLQKNFVDIVFERESKLYKDEGISTAELKYTSNKEVINVLCEKGKSVLS YLEDQCLAPGGTDEKFVSSCATNLKENNKFTPAKVASNKNFIIQHTIGPIQYCAESFLLK NKDVLRGDLVEVIKDSPNPIVQQLFEGQVIEKGKIAKGSLIGSQFLNQLTSLMNLINSTE PHFIRCIKPNENKKPLEWCEPKILIQLHALSILEALVLRQLGYSYRRTFEEFLYQYKFVD IAAAEDSSVENQNKCVNILKLSGLSESMYKIGKSMVFLKQEGAKILTKIQREKLVEWENC VSVIEAAILKHKYKQKVNKNIPSLLRVQAHIRKKMVAQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 5 |
| MG | Magnesium ion | Mg | 5 |
| 9UE | Jasplakinolide | C36 H45 Br N4 O6 | 3 |
The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity. Robert-Paganin, J., Xu, X.P., Swift, M.F. et al. Nat Commun (2021) 12:1892-1892. DOI 10.1038/s41467-021-22093-4 · PubMed
Other PDB entries of the same protein (UniProt Q8I4X0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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