Crystal structure of the kinesin-14 NcdG347D. Determined by X-ray diffraction at 2.35 Å resolution. Released 7 Mar 2012.
Explore 3U06 in 3D Show helices and sheets RCSB PDB PDBe
3U06 contains 33 α-helices and 34 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 | 293-345 | 53 | |
| β-strand | 349-355 | 7 | 1 |
| α-helix | 356-359 | 4 | |
| α-helix | 360-362 | 3 | |
| β-strand | 367 | 1 | 2 |
| β-strand | 369-374 | 6 | 3 |
| β-strand | 377-381 | 5 | 3 |
| β-strand | 395-397 | 3 | 3 |
| β-strand | 400-402 | 3 | 1 |
| α-helix | 408-412 | 5 | |
| 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 | 547-550 | 4 | |
| β-strand | 554-565 | 12 | 1 |
| β-strand | 570-580 | 11 | 1 |
| α-helix | 581-583 | 3 | |
| α-helix | 601-614 | 14 | |
| α-helix | 622-624 | 3 | |
| α-helix | 626-631 | 6 | |
| α-helix | 632-634 | 3 | |
| β-strand | 640-647 | 8 | 1 |
| β-strand | 650 | 1 | 2 |
| α-helix | 651-653 | 3 | |
| α-helix | 654-670 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 291-346 | 56 | |
| α-helix | 348-349 | 2 | |
| β-strand | 350-355 | 6 | 6 |
| α-helix | 356-359 | 4 | |
| α-helix | 361-364 | 4 | |
| β-strand | 367 | 1 | 7 |
| β-strand | 369-374 | 6 | 8 |
| β-strand | 377-381 | 5 | 8 |
| α-helix | 389-391 | 3 | |
| β-strand | 395-397 | 3 | 8 |
| β-strand | 400-402 | 3 | 6 |
| α-helix | 408-413 | 6 | |
| α-helix | 416-422 | 7 | |
| β-strand | 427-433 | 7 | 6 |
| α-helix | 440-444 | 5 | |
| β-strand | 446-447 | 2 | 9 |
| β-strand | 450-451 | 2 | 9 |
| α-helix | 453-471 | 19 | |
| β-strand | 474-485 | 12 | 6 |
| β-strand | 488-491 | 4 | 6 |
| β-strand | 520-521 | 2 | 6 |
| α-helix | 525-537 | 13 | |
| β-strand | 554-564 | 11 | 6 |
| β-strand | 571-580 | 10 | 6 |
| α-helix | 581-583 | 3 | |
| α-helix | 601-615 | 15 | |
| α-helix | 622-624 | 3 | |
| α-helix | 626-631 | 6 | |
| 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) |
>3U06_1 Protein claret segregational (chains A, B) MGSMHAALSTEVVHLRQRTEELLRCNEQQAAELETCKEQLFQSNMERKELHNTVMDLRDN IRVFCRIRPPLESEENRMCCTWTYHDESTVELQSIDAQAKSKMGQQIFSFDQVFHPLSSQ SDIFEMVSPLIQSALDGYNICIFAYGQTGSGKTYTMDGVPESVGVIPRTVDLLFDSIRGY RNLGWEYEIKATFLEIYNEVLYDLLSNEQKDMEIRMAKNNKNDIYVSNITEETVLDPNHL RHLMHTAKMNRATASTAGNERSSRSHAVTKLELIGRHAEKQEISVGSINLVDLAGSESPK TSTRMTETKNINRSLSELTNVILALLQKQDHIPYRNSKLTHLLMPSLGGNSKTLMFINVS PFQDCFQESVKSLRFAASVNSCKMTKAKRNRYLNNSVANSSTQSNNSGSFDK
Water and common crystallization additives (GOL) are not listed.
Neck-motor interactions trigger rotation of the kinesin stalk. Liu, H.L., Pemble Iv, C.W., Endow, S.A. Sci Rep (2012) 2:236-236. DOI 10.1038/srep00236 · 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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