Myosin VI D179Y (MD) pre-powerstroke state. Determined by X-ray diffraction at 1.95 Å resolution. Released 30 Jan 2013.
Explore 4DBR in 3D Show helices and sheets RCSB PDB PDBe
4DBR contains 47 α-helices and 32 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 |
|---|---|---|---|
| β-strand | 7-11 | 5 | 1 |
| β-strand | 15-24 | 10 | 1 |
| β-strand | 29-33 | 5 | 1 |
| β-strand | 41-43 | 3 | 1 |
| α-helix | 45-47 | 3 | |
| β-strand | 49-50 | 2 | 1 |
| β-strand | 61 | 1 | 2 |
| α-helix | 62-64 | 3 | |
| α-helix | 70-82 | 13 | |
| β-strand | 87-90 | 4 | 2 |
| β-strand | 93-97 | 5 | 2 |
| α-helix | 109-115 | 7 | |
| α-helix | 118-119 | 2 | |
| α-helix | 127-141 | 15 | |
| β-strand | 145-150 | 6 | 2 |
| β-strand | 152 | 1 | 3 |
| α-helix | 157-172 | 16 | |
| α-helix | 177-184 | 8 | |
| α-helix | 186-193 | 8 | |
| β-strand | 194-195 | 2 | 4 |
| β-strand | 203-204 | 2 | 4 |
| β-strand | 207-214 | 8 | 2 |
| β-strand | 220-228 | 9 | 2 |
| α-helix | 233-235 | 3 | |
| β-strand | 245 | 1 | 4 |
| α-helix | 246-254 | 9 | |
| α-helix | 257-263 | 7 | |
| α-helix | 268-270 | 3 | |
| α-helix | 272-275 | 4 | |
| α-helix | 280-281 | 2 | |
| β-strand | 282 | 1 | 5 |
| α-helix | 285-290 | 6 | |
| α-helix | 293-295 | 3 | |
| α-helix | 298-303 | 6 | |
| β-strand | 306 | 1 | 5 |
| α-helix | 313-327 | 15 | |
| α-helix | 331-348 | 18 | |
| β-strand | 352-354 | 3 | 6 |
| β-strand | 362-364 | 3 | 6 |
| α-helix | 366-368 | 3 | |
| α-helix | 369-378 | 10 | |
| α-helix | 383-391 | 9 | |
| β-strand | 392-393 | 2 | 7 |
| β-strand | 409-410 | 2 | 7 |
| α-helix | 413-440 | 28 | |
| β-strand | 450-456 | 7 | 2 |
| α-helix | 457-459 | 3 | |
| β-strand | 460 | 1 | 3 |
| α-helix | 468-484 | 17 | |
| α-helix | 485-491 | 7 | |
| α-helix | 492-498 | 7 | |
| α-helix | 503-505 | 3 | |
| α-helix | 512-519 | 8 | |
| α-helix | 525-533 | 9 | |
| α-helix | 540-550 | 11 | |
| β-strand | 557-558 | 2 | 8 |
| α-helix | 560-562 | 3 | |
| α-helix | 566-569 | 4 | |
| α-helix | 573-575 | 3 | |
| β-strand | 576-581 | 6 | 8 |
| β-strand | 584-589 | 6 | 8 |
| α-helix | 593-596 | 4 | |
| β-strand | 598 | 1 | 9 |
| α-helix | 603-610 | 8 | |
| α-helix | 615-620 | 6 | |
| β-strand | 642 | 1 | 9 |
| α-helix | 643-659 | 17 | |
| β-strand | 662-669 | 8 | 2 |
| α-helix | 682-691 | 10 | |
| α-helix | 694-700 | 7 | |
| β-strand | 707-710 | 4 | 10 |
| α-helix | 711-719 | 9 | |
| α-helix | 724-728 | 5 | |
| α-helix | 731-741 | 11 | |
| α-helix | 746-748 | 3 | |
| β-strand | 749-751 | 3 | 10 |
| β-strand | 755-758 | 4 | 10 |
| α-helix | 763-770 | 8 | |
| α-helix | 774-787 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Myosin-VI | A | protein | 786 | Sus scrofa | Q29122 (AlphaFold model) |
>4DBR_1 Myosin-VI (chains A) AKPVWAPHPTDGFQVGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVEDNC SLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSETIKSYQGKSLGTM PPHVFAIADKAFRDMKVLKLSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIYDRIV EANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKEER NYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYLKA GSLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGGCN LKNKSTQALEYCAELLGLDQDDLRVSLTTRVMLTTAGGAKGTVIKVPLKVEQANNARDAL AKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQQF FNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEARLVGILDILDEENRLPQPSDQHF TSAVHQKHKDHFRLSIPRKSKLAIHRNIRDDEGFIIRHFAGAVCYETTQFVEKNNDALHM SLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRSTGA SFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKYMP DKLARLDPRLFCKALFKALGLNEIDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELVKR VNHWLI
| ID | Name | Formula | Copies |
|---|---|---|---|
| VO4 | Vanadate ion | O4 V | 1 |
| MG | Magnesium ion | Mg | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
Water and common crystallization additives (EDO) are not listed.
Mutations in myosin VI that cause a loss of coordination between heads provide insights into the structural changes underlying force generation and the importance of gating. Song, L., Pylypenko, O., Yang, Z. et al. To be published.
Other PDB entries of the same protein (UniProt Q29122 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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