Cryo-EM structure of the kinesin-2 tail domain in complex with KAP3 and APC. Determined by electron microscopy at 2.9 Å resolution. Released 1 Oct 2025.
Explore 9W9I in 3D Show helices and sheets RCSB PDB PDBe
9W9I contains 70 α-helices and 6 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 |
|---|---|---|---|
| α-helix | 570-597 | 28 | |
| α-helix | 600-608 | 9 | |
| β-strand | 610-613 | 4 | 1 |
| β-strand | 618-621 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 563-590 | 28 | |
| α-helix | 593-602 | 10 | |
| β-strand | 603-606 | 4 | 2 |
| β-strand | 611-614 | 4 | 2 |
| α-helix | 624-629 | 6 | |
| α-helix | 641-649 | 9 | |
| α-helix | 653-655 | 3 | |
| α-helix | 663-665 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 140-143 | 4 | |
| α-helix | 149-161 | 13 | |
| α-helix | 163-165 | 3 | |
| α-helix | 166-171 | 6 | |
| α-helix | 176-183 | 8 | |
| α-helix | 192-197 | 6 | |
| α-helix | 201-205 | 5 | |
| α-helix | 210-217 | 8 | |
| α-helix | 219-244 | 26 | |
| α-helix | 245-247 | 3 | |
| β-strand | 254 | 1 | 3 |
| β-strand | 257 | 1 | 3 |
| α-helix | 260-288 | 29 | |
| α-helix | 293-301 | 9 | |
| α-helix | 304-311 | 8 | |
| α-helix | 317-331 | 15 | |
| α-helix | 334-341 | 8 | |
| α-helix | 346-350 | 5 | |
| α-helix | 358-371 | 14 | |
| α-helix | 375-384 | 10 | |
| α-helix | 386-393 | 8 | |
| α-helix | 400-411 | 12 | |
| α-helix | 414-420 | 7 | |
| α-helix | 428-435 | 8 | |
| α-helix | 443-452 | 10 | |
| α-helix | 456-462 | 7 | |
| α-helix | 467-477 | 11 | |
| α-helix | 481-490 | 10 | |
| α-helix | 496-500 | 5 | |
| α-helix | 501-504 | 4 | |
| α-helix | 505-511 | 7 | |
| α-helix | 521-529 | 9 | |
| α-helix | 539-544 | 6 | |
| α-helix | 548-554 | 7 | |
| α-helix | 562-574 | 13 | |
| α-helix | 580-587 | 8 | |
| 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 | 681-687 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 470-484 | 15 | |
| α-helix | 490-507 | 18 | |
| α-helix | 511-518 | 8 | |
| α-helix | 521-529 | 9 | |
| α-helix | 530-532 | 3 | |
| α-helix | 536-550 | 15 | |
| α-helix | 555-563 | 9 | |
| α-helix | 566-576 | 11 | |
| α-helix | 580-593 | 14 | |
| α-helix | 598-606 | 9 | |
| α-helix | 611-614 | 4 | |
| α-helix | 615-617 | 3 | |
| α-helix | 628-644 | 17 | |
| α-helix | 648-655 | 8 | |
| α-helix | 659-665 | 7 | |
| α-helix | 666-668 | 3 | |
| α-helix | 672-685 | 14 | |
| α-helix | 690-698 | 9 | |
| α-helix | 701-707 | 7 | |
| α-helix | 714-728 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinesin-like protein KIF3A | A | protein | 178 | Mus musculus | P28741 (AlphaFold model) |
| Kinesin-like protein KIF3B, N-terminally processed | B | protein | 220 | Mus musculus | Q61771 (AlphaFold model) |
| Kinesin-associated protein 3 | C | protein | 693 | Mus musculus | P70188 (AlphaFold model) |
| Adenomatous polyposis coli protein | D | protein | 680 | Mus musculus | Q61315 |
>9W9I_1 Kinesin-like protein KIF3A (chains A) MGSSHHHHHHSQSLQEEAQGKTKKLKKVWTMLMAAKSEMADLQQEHQREIEGLLENIRQL SRELRLQMLIIDNFIPQDYQEMIENYVHWNEDIGEWQLKCVAYTGNNMRKQTPVPDKKER DPFEVDLSHVYLAYTEESLRQSLMKLERPRTSKGKARPKMGRRKRSAKPETVIDSLLQ
>9W9I_2 Kinesin-like protein KIF3B, N-terminally processed (chains B) MSLQQEVDIKTKKLKKLFSKLQAVKAEIHDLQEEHIKERQELEQTQNELTRELKLKHLII ENFIPLEEKNKIMNRSFFDDEEDHWKLHPITRLENQQMMKRPVSAVGYKRPLSQHARMSM MIRPEPRYRAENIMLLELDMPSRTTRDYEGPAISPKVQAALDAALQDEDEIQVDASSFES TASRKPKARPKSGRKSGSSSSSSGNPASQFYPQSRGLVPK
>9W9I_3 Kinesin-associated protein 3 (chains C) MQGEDARYLKRKVKGGNIDVHPSEKALIVQYEVEATILGEMGDPMLGERKECQKIIRLKS LNANTDITSLARKVVEECKLIHPSKLSEVEQLLYYLQNRRDSLPGKEKKEKSSKPKDPPP FEGMEIDEVANINDMDEYIELLYEDIPDKVRGSALILQLARNPDNLEELLLNETALGALA RVLREDWKQSVELATNIIYIFFCFSSFSHFHGLITHYKIGALCMNIIDHELKRHELWQEE LSKKKKAVDEDLENQTLRKDYDKTFKKYQGLVVKQEQLLRVALYLLLNLAEDTRTELKMR NKNIVHMLVKALDRDNFELLILVVSFLKKLSIFMENKNDMVEMDIVEKLVKMIPCEHEDL LNITLRLLLNLSFDTGLRNKMVQVGLLPKLTALLGNENYKQIAMCVLYHISMDDRFKSMF AYTDCIPQLMKMLFECSDERIDLELISFCINLAANKRNVQLICEGNGLKMLMKRALKLKD PLLMKMIRNISQHDGPTKNLFIDYVGDLAAQISSDEEEEFVIECLGTLANLTIPDLDWEL VLKEYKLVPFLKDKLKPGAAEDDLVLEVVIMIGTVSMDDSCAALLAKSGIIPALIELLNA QQEDDEFVCQIIYVFYQMVFHQATRDVIIKETQAPAYLIDLMHDKNNEIRKVCDNTLDII AEYDEEWAKKIQSEKFRWHNSQWLEMVESRQLD
>9W9I_4 Adenomatous polyposis coli protein (chains D) MHHHHHHSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIH SQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEQGMDQDKNPMPAPVEHQICPAVCV LMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSVTLRRYAGMALTNLTFGD VANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKAL MECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAII ESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNP KDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSL HVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQNLYGDYAFDANRHDDSRSD NFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLSAYHPTTENAGT SSKRGLQITTTAAQIAKVMEEVSAIHTSQDDRSSASTTEFHCVADDRSAARRSSASHTHS NTYNFTKSENSNRTCSMPYAKVEYKRSSNDSLNSVTSSDGYGKRGQMKPSVESYSEDDES KFCSYGQYPADLAHKIHSAN
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:
MolViewer shows 9W9I directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.