Myosin VI motor domain in the Pi release state, space group P212121 - shortly soaked with PO4. Determined by X-ray diffraction at 2.0 Å resolution. Released 29 Apr 2015.
Explore 4PJN in 3D Show helices and sheets RCSB PDB PDBe
4PJN contains 48 α-helices and 33 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 | 15-25 | 11 | 1 |
| β-strand | 28-33 | 6 | 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 | |
| β-strand | 120 | 1 | 3 |
| β-strand | 123 | 1 | 3 |
| α-helix | 127-141 | 15 | |
| β-strand | 145-150 | 6 | 2 |
| 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 | 285-288 | 4 | |
| 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 | 352-355 | 4 | 6 |
| β-strand | 361-364 | 4 | 6 |
| α-helix | 366-368 | 3 | |
| α-helix | 369-379 | 11 | |
| α-helix | 383-391 | 9 | |
| β-strand | 392-394 | 3 | 7 |
| β-strand | 408-410 | 3 | 7 |
| α-helix | 411-412 | 2 | |
| α-helix | 413-442 | 30 | |
| β-strand | 450-456 | 7 | 2 |
| β-strand | 466 | 1 | 8 |
| 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 | 525-534 | 10 | |
| α-helix | 540-550 | 11 | |
| β-strand | 557-558 | 2 | 8 |
| α-helix | 560-562 | 3 | |
| α-helix | 566-568 | 3 | |
| 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 | 601-602 | 2 | |
| 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 | 694-702 | 9 | |
| β-strand | 707-710 | 4 | 10 |
| α-helix | 711-718 | 8 | |
| α-helix | 719-721 | 3 | |
| α-helix | 724-727 | 4 | |
| α-helix | 731-741 | 11 | |
| β-strand | 749-751 | 3 | 10 |
| β-strand | 755-758 | 4 | 10 |
| α-helix | 763-770 | 8 | |
| α-helix | 774-788 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Unconventional myosin-VI | A | protein | 788 | Sus scrofa | F1RQI7 (AlphaFold model) |
>4PJN_1 Unconventional myosin-VI (chains A) EDGKPVWAPHPTDGFQVGNIVDIGPDSLTIEPLNQKGKTFLALINQVFPAEEDSKKDVED NCSLMYLNEATLLHNIKVRYSKDRIYTYVANILIAVNPYFDIPKIYSSETIKSYQGKSLG TMPPHVFAIADKAFRDMKVLKLSQSIIVSGESGAGKTENTKFVLRYLTESYGTGQDIDDR IVEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHYLLEKSRICVQGKE ERNYHIFYRLCAGASEDIRERLHLSSPDNFRYLNRGCTRYFANKETDKQILQNRKSPEYL KAGSLKDPLLDDHGDFIRMCTAMKKIGLDDEEKLDLFRVVAGVLHLGNIDFEEAGSTSGG CNLKNKSTQALEYCAELLGLDQDDLRVSLTTRVMLTTAGGAKGTVIKVPLKVEQANNARD ALAKTVYSHLFDHVVNRVNQCFPFETSSYFIGVLDIAGFEYFEHNSFEQFCINYCNEKLQ QFFNERILKEEQELYQKEGLGVNEVHYVDNQDCIDLIEARLVGILDILDEENRLPQPSDQ HFTSAVHQKHKDHFRLSIPRKSKLAIHRNIRDDEGFIIRHFAGAVCYETTQFVEKNNDAL HMSLESLICESRDKFIRELFESSTNNNKDTKQKAGKLSFISVGNKFKTQLNLLLDKLRST GASFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRASFHELYNMYKKY MPDKLARLDPRLFCKALFKALGLNEIDYKFGLTKVFFRPGKFAEFDQIMKSDPDHLAELV KRVNHWLI
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 1 |
| PO4 | Phosphate ion | O4 P | 1 |
Water and common crystallization additives (GOL) are not listed.
How actin initiates the motor activity of Myosin. Llinas, P., Isabet, T., Song, L. et al. Dev Cell (2015) 33:401-412. DOI 10.1016/j.devcel.2015.03.025 · PubMed
Other PDB entries of the same protein (UniProt F1RQI7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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