KIF1A R350W bound to microtubules in the apo state. Determined by electron microscopy at 3.21 Å resolution. Released 22 Apr 2026.
Explore 9YAB in 3D Show helices and sheets RCSB PDB PDBe
9YAB contains 65 α-helices and 53 β-strands across 3 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 | 37-42 | 6 | |
| β-strand | 53-55 | 3 | 2 |
| β-strand | 61-63 | 3 | 2 |
| β-strand | 65-68 | 4 | 1 |
| β-strand | 69 | 1 | 3 |
| α-helix | 72-79 | 8 | |
| β-strand | 93 | 1 | 3 |
| α-helix | 103-104 | 2 | |
| α-helix | 105-109 | 5 | |
| α-helix | 115-128 | 14 | |
| β-strand | 132-138 | 7 | 1 |
| α-helix | 144-160 | 17 | |
| β-strand | 165-172 | 8 | 1 |
| α-helix | 173-174 | 2 | |
| α-helix | 183-189 | 7 | |
| α-helix | 191-192 | 2 | |
| α-helix | 193-197 | 5 | |
| β-strand | 200-205 | 6 | 1 |
| α-helix | 206-215 | 10 | |
| α-helix | 224-243 | 20 | |
| β-strand | 248 | 1 | 4 |
| α-helix | 252-259 | 8 | |
| β-strand | 269-272 | 4 | 4 |
| α-helix | 278-281 | 4 | |
| α-helix | 288-293 | 6 | |
| α-helix | 294-296 | 3 | |
| α-helix | 298-300 | 3 | |
| α-helix | 307-309 | 3 | |
| β-strand | 312-321 | 10 | 4 |
| α-helix | 325-336 | 12 | |
| β-strand | 343 | 1 | 4 |
| β-strand | 351-356 | 6 | 4 |
| β-strand | 373-381 | 9 | 4 |
| α-helix | 384-399 | 16 | |
| α-helix | 405-409 | 5 | |
| α-helix | 415-435 | 21 | |
| α-helix | 438-439 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-9 | 8 | 5 |
| α-helix | 10-28 | 19 | |
| β-strand | 30 | 1 | 6 |
| β-strand | 36 | 1 | 6 |
| α-helix | 42-45 | 4 | |
| α-helix | 47-49 | 3 | |
| β-strand | 51-53 | 3 | 7 |
| β-strand | 59-61 | 3 | 7 |
| β-strand | 63-67 | 5 | 5 |
| α-helix | 71-77 | 7 | |
| α-helix | 87-89 | 3 | |
| β-strand | 90-92 | 3 | 5 |
| α-helix | 101-102 | 2 | |
| α-helix | 103-107 | 5 | |
| α-helix | 109-126 | 18 | |
| β-strand | 129-138 | 10 | 5 |
| α-helix | 143 | 1 | |
| α-helix | 144-148 | 5 | |
| α-helix | 149-158 | 10 | |
| β-strand | 163-169 | 7 | 5 |
| α-helix | 181-195 | 15 | |
| β-strand | 198-202 | 5 | 5 |
| α-helix | 204-209 | 6 | |
| α-helix | 210-214 | 5 | |
| α-helix | 222-236 | 15 | |
| β-strand | 246 | 1 | 8 |
| α-helix | 250-257 | 8 | |
| β-strand | 265-266 | 2 | 5 |
| β-strand | 267-271 | 5 | 8 |
| α-helix | 286-294 | 9 | |
| α-helix | 296-298 | 3 | |
| α-helix | 305-307 | 3 | |
| β-strand | 310-319 | 10 | 8 |
| α-helix | 323-336 | 14 | |
| α-helix | 338-340 | 3 | |
| β-strand | 341 | 1 | 8 |
| β-strand | 349-354 | 6 | 8 |
| β-strand | 363-371 | 9 | 8 |
| α-helix | 374-389 | 16 | |
| α-helix | 396-399 | 4 | |
| α-helix | 405-424 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-12 | 7 | 9 |
| α-helix | 13-15 | 3 | |
| α-helix | 17-21 | 5 | |
| β-strand | 28-31 | 4 | 10 |
| β-strand | 34-37 | 4 | 10 |
| α-helix | 46-47 | 2 | |
| β-strand | 48-51 | 4 | 10 |
| β-strand | 54-57 | 4 | 9 |
| β-strand | 67 | 1 | 9 |
| α-helix | 70-73 | 4 | |
| α-helix | 74-78 | 5 | |
| α-helix | 79-87 | 9 | |
| β-strand | 91-96 | 6 | 9 |
| α-helix | 103-107 | 5 | |
| β-strand | 109 | 1 | 11 |
| β-strand | 116 | 1 | 11 |
| α-helix | 118-133 | 16 | |
| β-strand | 135 | 1 | 9 |
| β-strand | 138-150 | 13 | 9 |
| β-strand | 153-156 | 4 | 9 |
| α-helix | 164-165 | 2 | |
| β-strand | 166 | 1 | 9 |
| α-helix | 167 | 1 | |
| β-strand | 168-171 | 4 | 12 |
| β-strand | 175-178 | 4 | 12 |
| β-strand | 184-186 | 3 | 9 |
| α-helix | 189-202 | 14 | |
| β-strand | 205-206 | 2 | 13 |
| β-strand | 214-215 | 2 | 13 |
| β-strand | 218-230 | 13 | 9 |
| β-strand | 236-248 | 13 | 9 |
| α-helix | 249-252 | 4 | |
| α-helix | 263-289 | 27 | |
| α-helix | 299-301 | 3 | |
| α-helix | 310-314 | 5 | |
| α-helix | 316-319 | 4 | |
| β-strand | 324-331 | 8 | 9 |
| α-helix | 338-350 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin alpha-1B chain | A | protein | 451 | Sus scrofa | Q2XVP4 (AlphaFold model) |
| Tubulin beta-2B chain | B | protein | 445 | Sus scrofa | A0A8D1UIR5 (AlphaFold model) |
| Kinesin-like protein KIF1A | K | protein | 438 | Homo sapiens | Q12756 (AlphaFold model) |
>9YAB_1 Tubulin alpha-1B chain (chains A) MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE AREDMAALEKDYEEVGVDSVEGEGEEEGEEY
>9YAB_2 Tubulin beta-2B chain (chains B) MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEATGNKYV PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVV EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMM AACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS EYQQYQDATADEQGEFEEEEGEDEA
>9YAB_3 Kinesin-like protein KIF1A (chains K) MAGASVKVAVRVRPFNSREMSRDSKCIIQMSGSTTTIVNPKQPKETPKSFSFDYSYWSHT SPEDINYASQKQVYRDIGEEMLQHAFEGYNVCIFAYGQTGAGKSYTMMGKQEKDQQGIIP QLCEDLFSRINDTTNDNMSYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVED LSKLAVTSYNDIQDLMDSGNKARTVAATNMNETSSRSHAVFNIIFTQKRHDAETNITTEK VSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEMDSGPNKNKKKKK TDFIPYRDSVLTWLLRENLGGNSRTAMVAALSPADINYDETLSTLRYADWAKQIRCNAVI NEDPNNKLIRELKDEVTRLRDLLYAQGLGDITDGAGVKQLEDKVEELASKNYHLENEVAR LKKLVEFTSAWSHPQFEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| TA1 | Taxol | C47 H51 N O14 | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| MG | Magnesium ion | Mg | 1 |
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 1 |
Pathogenic KIF1A R350 mutations disrupt a conserved and conformation-dependent kinesin-tubulin salt bridge. Shatarupa, A., Rao, L., Asenjo, A.B. et al. Nat Commun (2026) 17. DOI 10.1038/s41467-026-71026-6 · 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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