S. pombe microtubule decorated with Cut7 motor domain in the AMPPNP state. Determined by electron microscopy at 4.5 Å resolution. Released 21 Aug 2019.
Explore 6S8M in 3D Show helices and sheets RCSB PDB PDBe
6S8M contains 55 α-helices and 54 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 | 1 | 11 |
| β-strand | 6-9 | 4 | 12 |
| α-helix | 10-27 | 18 | |
| β-strand | 57-58 | 2 | 13 |
| α-helix | 65 | 1 | |
| β-strand | 66-67 | 2 | 13 |
| β-strand | 71-73 | 3 | 12 |
| α-helix | 78-82 | 5 | |
| β-strand | 97-98 | 2 | 12 |
| α-helix | 107 | 1 | |
| α-helix | 108-113 | 6 | |
| α-helix | 114-119 | 6 | |
| α-helix | 123-131 | 9 | |
| β-strand | 136 | 1 | 11 |
| β-strand | 138-142 | 5 | 12 |
| β-strand | 144 | 1 | 14 |
| α-helix | 149-165 | 17 | |
| β-strand | 169-171 | 3 | 12 |
| β-strand | 175-176 | 2 | 14 |
| α-helix | 187-192 | 6 | |
| α-helix | 195-200 | 6 | |
| β-strand | 208-209 | 2 | 14 |
| α-helix | 212-218 | 7 | |
| α-helix | 228-240 | 13 | |
| α-helix | 243-246 | 4 | |
| α-helix | 256-262 | 7 | |
| β-strand | 273-277 | 5 | 15 |
| α-helix | 282-285 | 4 | |
| α-helix | 292-299 | 8 | |
| α-helix | 302-304 | 3 | |
| β-strand | 305 | 1 | 15 |
| β-strand | 316-325 | 10 | 15 |
| α-helix | 330-340 | 11 | |
| β-strand | 347 | 1 | 15 |
| β-strand | 357-359 | 3 | 15 |
| α-helix | 363-367 | 5 | |
| β-strand | 377-385 | 9 | 15 |
| α-helix | 389-403 | 15 | |
| α-helix | 410-413 | 4 | |
| α-helix | 420-439 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 5 |
| β-strand | 7-9 | 3 | 6 |
| α-helix | 11-28 | 18 | |
| α-helix | 42-45 | 4 | |
| β-strand | 51-52 | 2 | 7 |
| β-strand | 60-61 | 2 | 7 |
| β-strand | 64-67 | 4 | 6 |
| α-helix | 74 | 1 | |
| α-helix | 75-79 | 5 | |
| β-strand | 91-92 | 2 | 6 |
| α-helix | 101-103 | 3 | |
| α-helix | 104-108 | 5 | |
| α-helix | 109-125 | 17 | |
| β-strand | 130-134 | 5 | 5 |
| β-strand | 138 | 1 | 8 |
| α-helix | 143-147 | 5 | |
| α-helix | 148-158 | 11 | |
| β-strand | 163-166 | 4 | 5 |
| α-helix | 168 | 1 | |
| β-strand | 169-170 | 2 | 8 |
| α-helix | 171-172 | 2 | |
| α-helix | 181-194 | 14 | |
| β-strand | 198-200 | 3 | 5 |
| β-strand | 202-203 | 2 | 8 |
| α-helix | 204-211 | 8 | |
| α-helix | 222-236 | 15 | |
| β-strand | 244 | 1 | 9 |
| α-helix | 251-257 | 7 | |
| β-strand | 265-266 | 2 | 5 |
| β-strand | 267-271 | 5 | 9 |
| α-helix | 286-293 | 8 | |
| α-helix | 296-298 | 3 | |
| β-strand | 299 | 1 | 9 |
| β-strand | 310 | 1 | 10 |
| β-strand | 312-319 | 8 | 9 |
| α-helix | 323-336 | 14 | |
| β-strand | 341 | 1 | 10 |
| β-strand | 349-354 | 6 | 9 |
| β-strand | 363-370 | 8 | 9 |
| α-helix | 374-390 | 17 | |
| α-helix | 396-399 | 4 | |
| α-helix | 407-419 | 13 | |
| α-helix | 422-424 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 107-111 | 5 | 1 |
| α-helix | 117-123 | 7 | |
| β-strand | 141 | 1 | 2 |
| β-strand | 149 | 1 | 2 |
| β-strand | 158-159 | 2 | 1 |
| α-helix | 165-168 | 4 | |
| α-helix | 169-173 | 5 | |
| α-helix | 174-181 | 8 | |
| β-strand | 186-191 | 6 | 1 |
| α-helix | 198-202 | 5 | |
| α-helix | 219-231 | 13 | |
| β-strand | 240-247 | 8 | 1 |
| β-strand | 252-254 | 3 | 1 |
| β-strand | 268 | 1 | 3 |
| β-strand | 278 | 1 | 3 |
| β-strand | 285-287 | 3 | 1 |
| α-helix | 290-292 | 3 | |
| α-helix | 293-302 | 10 | |
| β-strand | 319-326 | 8 | 1 |
| β-strand | 328 | 1 | 4 |
| β-strand | 352 | 1 | 4 |
| β-strand | 356-359 | 4 | 1 |
| α-helix | 374-395 | 22 | |
| α-helix | 410-414 | 5 | |
| β-strand | 424-429 | 6 | 1 |
| α-helix | 446-450 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinesin-like protein cut7 | K | protein | 438 | Schizosaccharomyces pombe | P24339 (AlphaFold model) |
| Tubulin beta chain | B | protein | 448 | Schizosaccharomyces pombe | P05219 (AlphaFold model) |
| Tubulin alpha-1 chain | A | protein | 455 | Schizosaccharomyces pombe | P04688 (AlphaFold model) |
>6S8M_1 Kinesin-like protein cut7 (chains K) GIDPFTMAPRVAPGGSQQFLGKQGLKAKNPVSTPNSHFRSASNPRKRREPPTIDTGYPDR SDTNSPTDHALHDENETNINVVVRVRGRTDQEVRDNSSLAVSTSGAMGAELAIQSDPSSM LVTKTYAFDKVFGPEADQLMLFENSVAPMLEQVLNGYNCTIFAYGQTGTGKTYTMSGDLS DSDGILSEGAGLIPRALYQLFSSLDNSNQEYAVKCSYYELYNEEIRDLLVSEELRKPARV FEDTSRRGNVVITGIEESYIKNAGDGLRLLREGSHRRQVAATKCNDLSSRSHSIFTITLH RKVSSGMTDETNSLTINNNSDDLLRASKLHMVDLAGSENIGRSGAENKRARETGMINQSL LTLGRVINALVEKAHHIPYRESKLTRLLQDSLGGKTKTSMIVTVSSTNTNLEETISTLEY AARAKSIRNKPQNNQLVF
>6S8M_2 Tubulin beta chain (chains B) MREIVHIQAGQCGNQVGAAFWSTIADEHGLDSAGIYHGTSEAQHERLNVYFNEAAGGKYV PRAVLVDLEPGTMDAVKSGKFGNLFRPDNIIYGQSGAGNIWAKGHYTEGAELADAVLDVV RREAEACDALQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRMMATFSVAPAPKSSDTVV EPYNATLSMHQLVENSDETFCIDNEALSSIFANTLKIKSPSYDDLNHLVSAVMAGVTTSF RFPGELNSDLRKLAVNMVPFPRLHFFMVGFAPLAAIGSSSFQAVSVPELTQQMFDANNMM VAADPRHGRYLTVAALFRGKVSMKEVDEQIRSVQTKNSAYFVEWIPDNVLKAVCSVPPKD LKMSATFIGNSTSIQEIFRRLGDQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS EYQQYQEAGIDEGDEDYEIEEEKEPLEY
>6S8M_3 Tubulin alpha-1 chain (chains A) MREVISVHVGQAGVQIGNACWELYCLEHGIGPDGFPTENSEVHKNNSYLNDGFGTFFSET GQGKFVPRSIYVDLEPNVIDQVRTGPYKDLFHPEQMVTGKEDASNNYARGHYTVGKEMID SVLERIRRMADNCSGLQGFLVFHSFGGGTGSGLGALLLERLNMEYGKKSNLQFSVYPAPQ VSTSVVEPYNSVLTTHATLDNSDCTFMVDNEACYDICRRNLDIERPTYENLNRLIAQVVS SITASLRFAGSLNVDLNEFQTNLVPYPRIHFPLVTYSPIVSAAKAFHESNSVQEITNQCF EPYNQMVKCDPRTGRYMATCLLYRGDVIPRDVQAAVTSIKSRRTIQFVDWCPTGFKIGIC YEPPQHVPGSGIAKVNRAVCMLSNTTSIAEAWSRLDHKFDLMYSKRAFVHWYVGEGMEEG EFSEAREDLAALERDYEEVGQDSMDNEMYEADEEY
| ID | Name | Formula | Copies |
|---|---|---|---|
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 1 |
| EPB | 7,11-dihydroxy-8,8,10,12,16-pentamethyl-3-[1-methyl-2-(2-methyl-thiazol-4-yl)vi… | C27 H41 N O6 S | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
| MG | Magnesium ion | Mg | 1 |
Cryo-EM Structure (4.5- angstrom ) of Yeast Kinesin-5-Microtubule Complex Reveals a Distinct Binding Footprint and Mechanism of Drug Resistance. von Loeffelholz, O., Pena, A., Drummond, D.R. et al. J Mol Biol (2019) 431:864-872. DOI 10.1016/j.jmb.2019.01.011 · PubMed
Other PDB entries of the same protein (UniProt P24339 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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