The structure of kinesin-14 wild-type Ncd-ADP dimer. Determined by X-ray diffraction at 2.79 Å resolution. Released 20 Dec 2017.
Explore 5W3D in 3D Show helices and sheets RCSB PDB PDBe
5W3D contains 31 α-helices and 37 β-strands across 2 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 | 293-346 | 54 | |
| β-strand | 349-355 | 7 | 1 |
| α-helix | 356-359 | 4 | |
| α-helix | 366 | 1 | |
| β-strand | 367 | 1 | 2 |
| β-strand | 369-371 | 3 | 3 |
| β-strand | 377-381 | 5 | 3 |
| β-strand | 394-397 | 4 | 3 |
| β-strand | 400-402 | 3 | 1 |
| α-helix | 408-413 | 6 | |
| α-helix | 416-423 | 8 | |
| β-strand | 428-433 | 6 | 1 |
| α-helix | 440-444 | 5 | |
| β-strand | 446-447 | 2 | 4 |
| β-strand | 450-451 | 2 | 4 |
| α-helix | 453-468 | 16 | |
| α-helix | 469-471 | 3 | |
| β-strand | 473-485 | 13 | 1 |
| β-strand | 488-491 | 4 | 1 |
| β-strand | 502-504 | 3 | 5 |
| β-strand | 512-514 | 3 | 5 |
| β-strand | 520-521 | 2 | 1 |
| α-helix | 525-538 | 14 | |
| α-helix | 550-552 | 3 | |
| β-strand | 554-565 | 12 | 1 |
| β-strand | 570-580 | 11 | 1 |
| α-helix | 581-583 | 3 | |
| α-helix | 602-614 | 13 | |
| α-helix | 622-624 | 3 | |
| α-helix | 626-630 | 5 | |
| α-helix | 632-634 | 3 | |
| β-strand | 640-647 | 8 | 1 |
| β-strand | 650 | 1 | 2 |
| α-helix | 651-653 | 3 | |
| α-helix | 654-669 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 295-345 | 51 | |
| β-strand | 349-355 | 7 | 6 |
| α-helix | 356-359 | 4 | |
| α-helix | 366 | 1 | |
| β-strand | 367 | 1 | 7 |
| α-helix | 368 | 1 | |
| β-strand | 369-372 | 4 | 8 |
| β-strand | 377-381 | 5 | 8 |
| β-strand | 395-397 | 3 | 8 |
| β-strand | 400-402 | 3 | 6 |
| α-helix | 408-413 | 6 | |
| α-helix | 416-424 | 9 | |
| β-strand | 427-434 | 8 | 6 |
| α-helix | 440-444 | 5 | |
| β-strand | 446-447 | 2 | 9 |
| β-strand | 450-451 | 2 | 9 |
| α-helix | 453-468 | 16 | |
| β-strand | 474-479 | 6 | 10 |
| β-strand | 482-484 | 3 | 6 |
| β-strand | 489-491 | 3 | 6 |
| β-strand | 520-522 | 3 | 10 |
| α-helix | 525-538 | 14 | |
| β-strand | 554-556 | 3 | 6 |
| β-strand | 558 | 1 | 6 |
| β-strand | 561-564 | 4 | 10 |
| β-strand | 575-580 | 6 | 6 |
| α-helix | 581-583 | 3 | |
| α-helix | 601-614 | 14 | |
| α-helix | 627-630 | 4 | |
| β-strand | 641-647 | 7 | 6 |
| β-strand | 650 | 1 | 7 |
| α-helix | 651-653 | 3 | |
| α-helix | 654-667 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein claret segregational | A, B | protein | 412 | Drosophila melanogaster | P20480 (AlphaFold model) |
>5W3D_1 Protein claret segregational (chains A, B) MGSMHAALSTEVVHLRQRTEELLRCNEQQAAELETCKEQLFQSNMERKELHNTVMDLRGN IRVFCRIRPPLESEENRMCCTWTYHDESTVELQSIDAQAKSKMGQQIFSFDQVFHPLSSQ SDIFEMVSPLIQSALDGYNICIFAYGQTGSGKTYTMDGVPESVGVIPRTVDLLFDSIRGY RNLGWEYEIKATFLEIYNEVLYDLLSNEQKDMEIRMAKNNKNDIYVSNITEETVLDPNHL RHLMHTAKMNRATASTAGNERSSRSHAVTKLELIGRHAEKQEISVGSINLVDLAGSESPK TSTRMTETKNINRSLSELTNVILALLQKQDHIPYRNSKLTHLLMPSLGGNSKTLMFINVS PFQDCFQESVKSLRFAASVNSCKMTKAKRNRYLNNSVANSSTQSNNSGNFDK
Structural basis of small molecule ATPase inhibition of a human mitotic kinesin motor protein. Park, H.W., Ma, Z., Zhu, H. et al. Sci Rep (2017) 7:15121-15121. DOI 10.1038/s41598-017-14754-6 · PubMed
Other PDB entries of the same protein (UniProt P20480 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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