Nucleotide-free kinesin-1 motor domain bound to the microtubule. Determined by electron microscopy at 3.48 Å resolution. Released 23 Apr 2025.
Explore 9L7M in 3D Show helices and sheets RCSB PDB PDBe
9L7M contains 108 α-helices and 99 β-strands across 5 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 | 3-9 | 7 | 1 |
| α-helix | 10-27 | 18 | |
| α-helix | 50-52 | 3 | |
| β-strand | 55-56 | 2 | 2 |
| β-strand | 60-61 | 2 | 2 |
| β-strand | 65-68 | 4 | 1 |
| α-helix | 75-80 | 6 | |
| α-helix | 104 | 1 | |
| α-helix | 105-109 | 5 | |
| α-helix | 115-123 | 9 | |
| β-strand | 132-138 | 7 | 1 |
| β-strand | 139-140 | 2 | 3 |
| α-helix | 145-149 | 5 | |
| α-helix | 150-159 | 10 | |
| β-strand | 165-167 | 3 | 1 |
| β-strand | 169-171 | 3 | 3 |
| α-helix | 183-189 | 7 | |
| α-helix | 193-196 | 4 | |
| β-strand | 202-204 | 3 | 3 |
| α-helix | 207-211 | 5 | |
| α-helix | 212-216 | 5 | |
| α-helix | 224-233 | 10 | |
| α-helix | 235-238 | 4 | |
| β-strand | 248 | 1 | 4 |
| α-helix | 254-259 | 6 | |
| β-strand | 269-270 | 2 | 5 |
| β-strand | 273 | 1 | 6 |
| α-helix | 288-291 | 4 | |
| α-helix | 294-296 | 3 | |
| β-strand | 312 | 1 | 7 |
| β-strand | 317-318 | 2 | 8 |
| β-strand | 320-321 | 2 | 9 |
| α-helix | 327-337 | 11 | |
| β-strand | 343 | 1 | 7 |
| β-strand | 353-354 | 2 | 8 |
| β-strand | 355 | 1 | 4 |
| α-helix | 359-360 | 2 | |
| β-strand | 373-374 | 2 | 9 |
| β-strand | 375 | 1 | 6 |
| β-strand | 377 | 1 | 8 |
| β-strand | 378-379 | 2 | 5 |
| β-strand | 381 | 1 | 7 |
| α-helix | 383-386 | 4 | |
| α-helix | 388-392 | 5 | |
| α-helix | 405-409 | 5 | |
| α-helix | 416-434 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-9 | 6 | 10 |
| α-helix | 11-27 | 17 | |
| β-strand | 30 | 1 | 11 |
| β-strand | 36 | 1 | 11 |
| α-helix | 43-47 | 3 | |
| α-helix | 49-51 | 3 | |
| β-strand | 53-56 | 4 | 12 |
| β-strand | 60-63 | 4 | 12 |
| β-strand | 65-69 | 5 | 10 |
| α-helix | 74-80 | 7 | |
| β-strand | 93-94 | 2 | 10 |
| α-helix | 104-107 | 4 | |
| α-helix | 116-122 | 7 | |
| β-strand | 134-140 | 7 | 10 |
| α-helix | 145-150 | 6 | |
| α-helix | 151-157 | 7 | |
| β-strand | 165-166 | 2 | 10 |
| β-strand | 169-172 | 4 | 10 |
| α-helix | 175-177 | 3 | |
| α-helix | 183-194 | 12 | |
| β-strand | 201-205 | 5 | 10 |
| α-helix | 206-214 | 9 | |
| α-helix | 224-226 | 3 | |
| α-helix | 228-238 | 11 | |
| β-strand | 248 | 1 | 13 |
| α-helix | 252-258 | 7 | |
| β-strand | 267-268 | 2 | 10 |
| β-strand | 269-273 | 5 | 13 |
| α-helix | 281-283 | 3 | |
| α-helix | 288-294 | 7 | |
| α-helix | 298-300 | 3 | |
| α-helix | 307-309 | 3 | |
| β-strand | 312-320 | 9 | 13 |
| α-helix | 325-337 | 13 | |
| β-strand | 343 | 1 | 13 |
| β-strand | 351-355 | 5 | 13 |
| α-helix | 359 | 1 | |
| β-strand | 374-381 | 8 | 13 |
| α-helix | 382-385 | 4 | |
| α-helix | 387-396 | 10 | |
| α-helix | 399-401 | 3 | |
| α-helix | 406-409 | 4 | |
| α-helix | 416-423 | 8 | |
| α-helix | 427-433 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-15 | 7 | 27 |
| α-helix | 21-25 | 5 | |
| α-helix | 27-29 | 3 | |
| β-strand | 33-34 | 2 | 28 |
| β-strand | 38-41 | 4 | 28 |
| β-strand | 44-47 | 4 | 28 |
| β-strand | 51-52 | 2 | 27 |
| α-helix | 58-65 | 8 | |
| α-helix | 71-74 | 4 | |
| β-strand | 79-85 | 7 | 27 |
| α-helix | 91-94 | 4 | |
| β-strand | 97 | 1 | 29 |
| β-strand | 105 | 1 | 29 |
| α-helix | 109-120 | 12 | |
| β-strand | 126-138 | 13 | 27 |
| β-strand | 141-144 | 4 | 27 |
| β-strand | 153 | 1 | 27 |
| β-strand | 155-156 | 2 | 30 |
| β-strand | 164-165 | 2 | 30 |
| β-strand | 171-173 | 3 | 27 |
| α-helix | 176-187 | 12 | |
| β-strand | 205-216 | 12 | 27 |
| β-strand | 222-231 | 10 | 27 |
| α-helix | 246-270 | 25 | |
| α-helix | 281-286 | 6 | |
| β-strand | 295-302 | 8 | 27 |
| α-helix | 309-321 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin alpha-1B chain | A, C | protein | 451 | Sus scrofa | Q2XVP4 (AlphaFold model) |
| Tubulin beta chain | B, D | protein | 445 | Sus scrofa | P02554 (AlphaFold model) |
| Kinesin-1 heavy chain | K | protein | 357 | Homo sapiens | P33176 (AlphaFold model) |
>9L7M_1 Tubulin alpha-1B chain (chains A, C) MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE AREDMAALEKDYEEVGVDSVEGEGEEEGEEY
>9L7M_2 Tubulin beta chain (chains B, D) MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS EYQQYQDATADEQGEFEEEGEEDEA
>9L7M_3 Kinesin-1 heavy chain (chains K) MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQ VYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIY SMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVM DTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSK TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVI CCSPSSYNESETKSTLLFGQRAKTIKNTVSVNVELTAEQWKKKYEKCKEGTHHHHHH
Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping. Makino, T., Kanada, R., Mori, T. et al. J Cell Biol (2025) 224. DOI 10.1083/jcb.202501253 · 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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