Kinesin-14 with AlF3 bound to 14 PF Microtubule. Determined by electron microscopy at 3.99 Å resolution. Released 8 Oct 2025.
Explore 8YY5 in 3D Show helices and sheets RCSB PDB PDBe
8YY5 contains 78 α-helices and 71 β-strands across 4 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 | 5-8 | 4 | 1 |
| α-helix | 11-28 | 18 | |
| β-strand | 53-55 | 3 | 2 |
| β-strand | 61-63 | 3 | 2 |
| β-strand | 65-67 | 3 | 1 |
| β-strand | 68 | 1 | 3 |
| α-helix | 72-80 | 9 | |
| α-helix | 82-84 | 3 | |
| β-strand | 93 | 1 | 3 |
| α-helix | 103-104 | 2 | |
| α-helix | 105-109 | 5 | |
| α-helix | 111-128 | 18 | |
| β-strand | 135-140 | 6 | 1 |
| α-helix | 144 | 1 | |
| α-helix | 145-149 | 5 | |
| α-helix | 150-160 | 11 | |
| β-strand | 167-172 | 6 | 1 |
| α-helix | 173-174 | 2 | |
| α-helix | 183-192 | 10 | |
| β-strand | 200-205 | 6 | 1 |
| α-helix | 206-215 | 10 | |
| α-helix | 224-238 | 15 | |
| α-helix | 240-243 | 4 | |
| α-helix | 252-259 | 8 | |
| α-helix | 268 | 1 | |
| β-strand | 269-272 | 4 | 1 |
| α-helix | 278-283 | 6 | |
| α-helix | 288-294 | 7 | |
| α-helix | 311 | 1 | |
| β-strand | 312-321 | 10 | 1 |
| α-helix | 325-337 | 13 | |
| β-strand | 343 | 1 | 1 |
| β-strand | 353 | 1 | 1 |
| α-helix | 359-361 | 3 | |
| α-helix | 369-370 | 2 | |
| β-strand | 373-381 | 9 | 1 |
| α-helix | 383-400 | 18 | |
| α-helix | 405-409 | 5 | |
| α-helix | 415-436 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 4 |
| α-helix | 10-28 | 19 | |
| β-strand | 30 | 1 | 5 |
| β-strand | 35 | 1 | 6 |
| β-strand | 36 | 1 | 5 |
| α-helix | 41-44 | 4 | |
| α-helix | 47-49 | 3 | |
| β-strand | 51-55 | 5 | 6 |
| β-strand | 58-61 | 4 | 6 |
| β-strand | 63-66 | 4 | 4 |
| α-helix | 70-78 | 9 | |
| α-helix | 87-89 | 3 | |
| β-strand | 90 | 1 | 4 |
| α-helix | 101-106 | 6 | |
| α-helix | 108-126 | 19 | |
| β-strand | 130-131 | 2 | 4 |
| β-strand | 132 | 1 | 7 |
| β-strand | 133-136 | 4 | 4 |
| α-helix | 142-158 | 17 | |
| β-strand | 163 | 1 | 7 |
| α-helix | 170-172 | 3 | |
| α-helix | 181-195 | 15 | |
| β-strand | 199-200 | 2 | 8 |
| α-helix | 204-209 | 6 | |
| α-helix | 210-214 | 5 | |
| α-helix | 222-241 | 20 | |
| α-helix | 250-256 | 7 | |
| β-strand | 265-266 | 2 | 8 |
| β-strand | 267 | 1 | 9 |
| β-strand | 271 | 1 | 10 |
| α-helix | 286-291 | 6 | |
| α-helix | 296-298 | 3 | |
| α-helix | 305-307 | 3 | |
| β-strand | 310-313 | 4 | 9 |
| β-strand | 318 | 1 | 11 |
| β-strand | 319 | 1 | 12 |
| α-helix | 323-336 | 14 | |
| β-strand | 341 | 1 | 9 |
| β-strand | 354 | 1 | 11 |
| α-helix | 357-358 | 2 | |
| β-strand | 363 | 1 | 12 |
| β-strand | 365 | 1 | 10 |
| β-strand | 369-371 | 3 | 9 |
| α-helix | 375-390 | 16 | |
| α-helix | 396-400 | 5 | |
| α-helix | 405-427 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 326-346 | 21 | |
| β-strand | 350-355 | 6 | 13 |
| α-helix | 356-359 | 4 | |
| α-helix | 360-365 | 6 | |
| β-strand | 371-374 | 4 | 14 |
| β-strand | 377-379 | 3 | 14 |
| α-helix | 386-390 | 5 | |
| β-strand | 395-397 | 3 | 14 |
| β-strand | 400-402 | 3 | 13 |
| α-helix | 408-412 | 5 | |
| α-helix | 416-425 | 10 | |
| β-strand | 427-434 | 8 | 13 |
| α-helix | 440-443 | 4 | |
| α-helix | 453-469 | 17 | |
| β-strand | 474-485 | 12 | 13 |
| β-strand | 488-491 | 4 | 13 |
| β-strand | 501-504 | 4 | 15 |
| β-strand | 512-515 | 4 | 15 |
| β-strand | 519-521 | 3 | 13 |
| α-helix | 525-541 | 17 | |
| α-helix | 550-552 | 3 | |
| β-strand | 554-565 | 12 | 13 |
| β-strand | 570-583 | 14 | 13 |
| α-helix | 593-615 | 23 | |
| α-helix | 626-630 | 5 | |
| α-helix | 632-636 | 5 | |
| β-strand | 639-647 | 9 | 13 |
| α-helix | 654-668 | 15 | |
| α-helix | 672-675 | 4 | |
| β-strand | 678-681 | 4 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 326-346 | 21 | |
| β-strand | 350-355 | 6 | 16 |
| α-helix | 356-358 | 3 | |
| β-strand | 367 | 1 | 17 |
| β-strand | 369-371 | 3 | 18 |
| β-strand | 377-381 | 5 | 18 |
| α-helix | 385-388 | 4 | |
| β-strand | 395-397 | 3 | 18 |
| β-strand | 400-402 | 3 | 16 |
| α-helix | 408-412 | 5 | |
| α-helix | 416-422 | 7 | |
| β-strand | 427-433 | 7 | 16 |
| α-helix | 440-444 | 5 | |
| β-strand | 446 | 1 | 19 |
| β-strand | 451 | 1 | 19 |
| α-helix | 453-468 | 16 | |
| α-helix | 469-471 | 3 | |
| β-strand | 473-484 | 12 | 16 |
| β-strand | 489-491 | 3 | 16 |
| β-strand | 502-504 | 3 | 20 |
| β-strand | 512-514 | 3 | 20 |
| β-strand | 520-522 | 3 | 16 |
| α-helix | 525-539 | 15 | |
| α-helix | 550-552 | 3 | |
| β-strand | 554-565 | 12 | 16 |
| β-strand | 569-580 | 12 | 16 |
| α-helix | 581-583 | 3 | |
| α-helix | 600-614 | 15 | |
| α-helix | 622-624 | 3 | |
| α-helix | 626-630 | 5 | |
| α-helix | 632-635 | 4 | |
| β-strand | 640-647 | 8 | 16 |
| β-strand | 650 | 1 | 17 |
| α-helix | 654-668 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin alpha-1B chain | A | protein | 451 | Sus scrofa | Q2XVP4 (AlphaFold model) |
| Tubulin beta chain | B | protein | 444 | Sus scrofa | Q767L7 (AlphaFold model) |
| Protein claret segregational | C, D | protein | 409 | Drosophila melanogaster | P20480 (AlphaFold model) |
>8YY5_1 Tubulin alpha-1B chain (chains A) MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE AREDMAALEKDYEEVGVDSVEGEGEEEGEEY
>8YY5_2 Tubulin beta chain (chains B) MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYV PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMM AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS EYQQYQDATAEEEEDFGEEAEEEA
>8YY5_3 Protein claret segregational (chains C, D) MHAALSTEVVHLRQRTEELLRCNEQQAAELETCKEQLFQSNMERKELHNTVMDLRGNIRV FCRIRPPLESEENRMCCTWTYHDESTVELQSIDAQAKSKMGQQIFSFDQVFHPLSSQSDI FEMVSPLIQSALDGYNICIFAYGQTGSGKTYTMDGVPESVGVIPRTVDLLFDSIRGYRNL GWEYEIKATFLEIKNEVLYDLLSNEQKDMEIRMAKNNKNDIYVSNITEETVLDPNHLRHL MHTAKMNRATASTAGNERSSRSHAVTKLELIGRHAEKQEISVGSINLVDLAGSESPKTST RMTETKNINRSLSELTNVILALLQKQDHIPYRNSKLTHLLMPSLGGNSKTLMFINVSPFQ DCFQESVKSLRFAASVNSCKMTKAKRNRYLNNSVANSSTQSNNSGNFDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ALF | Tetrafluoroaluminate ion | Al F4 | 1 |
| MG | Magnesium ion | Mg | 2 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 1 |
Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility. Shibata, S., Wang, M.Y., Imasaki, T. et al. Sci Rep (2026) 16:487-487. DOI 10.1038/s41598-025-28573-7 · PubMed
Other PDB entries of the same protein (UniProt Q2XVP4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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