Cryo-EM structure of the mouse kinesin-2 tail in complex with KAP3 adaptor. Determined by electron microscopy at 2.83 Å resolution. Released 1 Oct 2025.
Explore 9W9H in 3D Show helices and sheets RCSB PDB PDBe
9W9H contains 53 α-helices and 10 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 |
|---|---|---|---|
| α-helix | 581-597 | 17 | |
| α-helix | 600-608 | 9 | |
| β-strand | 610-613 | 4 | 1 |
| β-strand | 618-621 | 4 | 1 |
| α-helix | 624-626 | 3 | |
| α-helix | 628-634 | 7 | |
| α-helix | 651-653 | 3 | |
| β-strand | 655 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 575-589 | 15 | |
| α-helix | 593-601 | 9 | |
| β-strand | 604-606 | 3 | 3 |
| β-strand | 611-613 | 3 | 3 |
| α-helix | 625-629 | 5 | |
| α-helix | 641-649 | 9 | |
| α-helix | 653-655 | 3 | |
| α-helix | 667-670 | 4 | |
| β-strand | 673 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 140-143 | 4 | |
| α-helix | 149-160 | 12 | |
| α-helix | 166-171 | 6 | |
| α-helix | 176-185 | 10 | |
| α-helix | 193-195 | 3 | |
| α-helix | 201-205 | 5 | |
| β-strand | 207 | 1 | 4 |
| α-helix | 208-210 | 3 | |
| α-helix | 211-216 | 6 | |
| α-helix | 219-243 | 25 | |
| β-strand | 254 | 1 | 5 |
| β-strand | 257 | 1 | 5 |
| α-helix | 259-289 | 31 | |
| α-helix | 293-300 | 8 | |
| α-helix | 304-311 | 8 | |
| α-helix | 317-330 | 14 | |
| β-strand | 333 | 1 | 2 |
| α-helix | 334-342 | 9 | |
| α-helix | 346-349 | 4 | |
| α-helix | 358-371 | 14 | |
| α-helix | 375-383 | 9 | |
| α-helix | 386-392 | 7 | |
| α-helix | 400-411 | 12 | |
| α-helix | 414-416 | 3 | |
| α-helix | 418-420 | 3 | |
| α-helix | 427-435 | 9 | |
| α-helix | 443-452 | 10 | |
| α-helix | 456-462 | 7 | |
| α-helix | 468-477 | 10 | |
| α-helix | 481-491 | 11 | |
| α-helix | 496-499 | 4 | |
| α-helix | 502-504 | 3 | |
| α-helix | 505-512 | 8 | |
| α-helix | 519-529 | 11 | |
| α-helix | 538-544 | 7 | |
| α-helix | 547-553 | 7 | |
| α-helix | 562-575 | 14 | |
| α-helix | 582-588 | 7 | |
| α-helix | 590-600 | 11 | |
| α-helix | 605-619 | 15 | |
| α-helix | 624-626 | 3 | |
| α-helix | 627-631 | 5 | |
| α-helix | 634-640 | 7 | |
| α-helix | 647-663 | 17 | |
| α-helix | 665-679 | 15 | |
| α-helix | 681-685 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinesin-like protein KIF3A | A | protein | 233 | Mus musculus | P28741 (AlphaFold model) |
| Kinesin-like protein KIF3B | B | protein | 273 | Mus musculus | Q61771 (AlphaFold model) |
| Kinesin-associated protein 3 | C | protein | 693 | Mus musculus | P70188 (AlphaFold model) |
>9W9H_1 Kinesin-like protein KIF3A (chains A) MGSSHHHHHHSQVIVGGVDLLAKAEEQEKLLEESNMELEERRRRAEQLRKELEEKEQERL DIEEKYTSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQLSRELR LQMLIIDNFIPQDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKERDPFEV DLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKMGRRKRSAKPETVIDSLLQ
>9W9H_2 Kinesin-like protein KIF3B (chains B) LVGGKNIVDHTNEQQKILEQKRQEIAEQKRREREIQQQMESRDEETLELKETYTSLQQEV DIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLIIENFIPLE EKNKIMNRSFFDDEEDHWKLHPITRLENQQMMKRPVSAVGYKRPLSQHARMSMMIRPEPR YRAENIMLLELDMPSRTTRDYEGPAISPKVQAALDAALQDEDEIQVDASSFESTASRKPK ARPKSGRKSGSSSSSSGNPASQFYPQSRGLVPK
>9W9H_3 Kinesin-associated protein 3 (chains C) MQGEDARYLKRKVKGGNIDVHPSEKALIVQYEVEATILGEMGDPMLGERKECQKIIRLKS LNANTDITSLARKVVEECKLIHPSKLSEVEQLLYYLQNRRDSLPGKEKKEKSSKPKDPPP FEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELLLNETALGALA RVLREDWKQSVELATNIIYIFFCFSSFSHFHGLITHYKIGALCMNIIDHELKRHELWQEE LSKKKKAVDEDLENQTLRKDYDKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMR NKNIVHMLVKALDRDNFELLILVVSFLKKLSIFMENKNDMVEMDIVEKLVKMIPCEHEDL LNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNENYKQIAMCVLYHISMDDRFKSMF AYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKLKD PLLMKMIRNISQHDGPTKNLFIDYVGDLAAQISSDEEEEFVIECLGTLANLTIPDLDWEL VLKEYKLVPFLKDKLKPGAAEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIPALIELLNA QQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNNEIRKVCDNTLDII AEYDEEWAKKIQSEKFRWHNSQWLEMVESRQLD
The hook-like adaptor and cargo-binding (HAC) domain in the kinesin-2 tail enables adaptor assembly and cargo recognition. Jiang, X., Danev, R., Ichinose, S. et al. Sci Adv (2025) 11:eady5861-eady5861. DOI 10.1126/sciadv.ady5861 · PubMed
Other PDB entries of the same protein (UniProt P28741 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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