CryoEM structure of primed myosin-5a (ADP-Pi state). Determined by electron microscopy at 4.9 Å resolution. Released 11 Dec 2024.
Explore 8RBG in 3D Show helices and sheets RCSB PDB PDBe
8RBG contains 41 α-helices and 29 β-strands across 1 chain. 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 |
|---|---|---|---|
| α-helix | 3-6 | 4 | |
| β-strand | 12-17 | 6 | 1 |
| β-strand | 21-27 | 7 | 1 |
| β-strand | 37-42 | 6 | 1 |
| β-strand | 47-51 | 5 | 1 |
| α-helix | 52-53 | 2 | |
| α-helix | 58-60 | 3 | |
| β-strand | 61-62 | 2 | 1 |
| α-helix | 63-65 | 3 | |
| α-helix | 66-68 | 3 | |
| β-strand | 73 | 1 | 2 |
| α-helix | 74-76 | 3 | |
| α-helix | 82-94 | 13 | |
| β-strand | 100-103 | 4 | 2 |
| β-strand | 106-110 | 5 | 2 |
| α-helix | 121-127 | 7 | |
| α-helix | 130-131 | 2 | |
| β-strand | 132 | 1 | 3 |
| β-strand | 135 | 1 | 3 |
| α-helix | 139-153 | 15 | |
| β-strand | 157-162 | 6 | 2 |
| β-strand | 164 | 1 | 4 |
| α-helix | 169-184 | 16 | |
| α-helix | 191-207 | 17 | |
| β-strand | 208-209 | 2 | 5 |
| β-strand | 217-218 | 2 | 5 |
| β-strand | 221-228 | 8 | 2 |
| β-strand | 234-242 | 9 | 2 |
| α-helix | 247-250 | 4 | |
| α-helix | 260-267 | 8 | |
| α-helix | 272-277 | 6 | |
| α-helix | 282-284 | 3 | |
| α-helix | 286-289 | 4 | |
| α-helix | 301-315 | 15 | |
| α-helix | 319-336 | 18 | |
| β-strand | 341-343 | 3 | 6 |
| β-strand | 347-349 | 3 | 6 |
| α-helix | 355-364 | 10 | |
| α-helix | 368-376 | 9 | |
| β-strand | 377-381 | 5 | 7 |
| β-strand | 386-390 | 5 | 7 |
| α-helix | 393-423 | 31 | |
| β-strand | 431-437 | 7 | 2 |
| α-helix | 439-440 | 2 | |
| β-strand | 441 | 1 | 4 |
| α-helix | 449-466 | 18 | |
| α-helix | 467-472 | 6 | |
| α-helix | 473-480 | 8 | |
| α-helix | 493-500 | 8 | |
| α-helix | 505-514 | 10 | |
| α-helix | 520-531 | 12 | |
| β-strand | 538-539 | 2 | 8 |
| β-strand | 547-551 | 5 | 8 |
| β-strand | 556-560 | 5 | 8 |
| α-helix | 564-569 | 6 | |
| α-helix | 574-581 | 8 | |
| α-helix | 587-592 | 6 | |
| α-helix | 635-652 | 18 | |
| β-strand | 654-661 | 8 | 2 |
| α-helix | 674-684 | 11 | |
| α-helix | 686-695 | 10 | |
| β-strand | 699-702 | 4 | 9 |
| α-helix | 703-710 | 8 | |
| α-helix | 711-713 | 3 | |
| α-helix | 716-718 | 3 | |
| α-helix | 723-734 | 12 | |
| α-helix | 738-740 | 3 | |
| β-strand | 741-743 | 3 | 9 |
| β-strand | 747-750 | 4 | 9 |
| α-helix | 754-777 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Unconventional myosin-Va | A | protein | 801 | Mus musculus | Q99104 (AlphaFold model) |
>8RBG_1 Unconventional myosin-Va (chains A) MAASELYTKFARVWIPDPEEVWKSAELLKDYKPGDKVLLLHLEEGKDLEYRLDPKTGELP HLRNPDILVGENDLTALSYLHEPAVLHNLRVRFIDSKLIYTYCGIVLVAINPYEQLPIYG EDIINAYSGQNMGDMDPHIFAVAEEAYKQMARDERNQSIIVSGESGAGKTVSAKYAMRYF ATVSGSASEANVEEKVLASNPIMESIGNAKTTRNDNASRFGKYIEIGFDKRYRIIGANMR TYLLEKSRVVFQAEEERNYHIFYQLCASAKLPEFKMLRLGNADSFHYTKQGGSPMIEGVD DAKEMAHTRQACTLLGISESYQMGIFRILAGILHLGNVGFASRDSDSCTIPPKHEPLTIF CDLMGVDYEEMCHWLCHRKLATATETYIKPISKLQATNARDALAKHIYAKLFNWIVDHVN QALHSAVKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNMHVFKLEQEEYMKE QIPWTLIDFYDNQPCINLIESKLGILDLLDEECKMPKGTDDTWAQKLYNTHLNKCALFEK PRMSNKAFIIKHFADKVEYQCEGFLEKNKDTVFEEQIKVLKSSKFKMLPELFQAISPTSA TSSGRTPLTRVPVKPTKGRPGQTAKEHKKTVGHQFRNSLHLLMETLNATTPHYVRCIKPN DFKFPFTFDEKRAVQQLRACGVLETIRISAAGFPSRWTYQEFFSRYRVLMKQKDVLGDRK QTCKNVLEKLILDKDKYQFGKTKIFFRAGQVAYLEKLRADKLRAACIRIQKTIRGWLLRK RYLCMQRAAITVQDYKDDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| MG | Magnesium ion | Mg | 1 |
| PO4 | Phosphate ion | O4 P | 1 |
Swinging lever mechanism of myosin directly shown by time-resolved cryo-EM. Klebl, D.P., McMillan, S.N., Risi, C. et al. Nature (2025) 642:519-526. DOI 10.1038/s41586-025-08876-5 · PubMed
Other PDB entries of the same protein (UniProt Q99104 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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