6S8M: Kinesin-like protein cut7

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.

Method
Electron microscopy
Resolution
4.5 Å
Organism
Schizosaccharomyces pombe
Chains
3
Atoms
9,480
Mol. weight
150.95 kDa
Ligands
GTP, EPB, GDP, ANP
Released
21 Aug 2019

Explore 6S8M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 22 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand3111
β-strand6-9412
α-helix10-2718
β-strand57-58213
α-helix651
β-strand66-67213
β-strand71-73312
α-helix78-825
β-strand97-98212
α-helix1071
α-helix108-1136
α-helix114-1196
α-helix123-1319
β-strand136111
β-strand138-142512
β-strand144114
α-helix149-16517
β-strand169-171312
β-strand175-176214
α-helix187-1926
α-helix195-2006
β-strand208-209214
α-helix212-2187
α-helix228-24013
α-helix243-2464
α-helix256-2627
β-strand273-277515
α-helix282-2854
α-helix292-2998
α-helix302-3043
β-strand305115
β-strand316-3251015
α-helix330-34011
β-strand347115
β-strand357-359315
α-helix363-3675
β-strand377-385915
α-helix389-40315
α-helix410-4134
α-helix420-43920
Chain B: 22 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand3-645
β-strand7-936
α-helix11-2818
α-helix42-454
β-strand51-5227
β-strand60-6127
β-strand64-6746
α-helix741
α-helix75-795
β-strand91-9226
α-helix101-1033
α-helix104-1085
α-helix109-12517
β-strand130-13455
β-strand13818
α-helix143-1475
α-helix148-15811
β-strand163-16645
α-helix1681
β-strand169-17028
α-helix171-1722
α-helix181-19414
β-strand198-20035
β-strand202-20328
α-helix204-2118
α-helix222-23615
β-strand24419
α-helix251-2577
β-strand265-26625
β-strand267-27159
α-helix286-2938
α-helix296-2983
β-strand29919
β-strand310110
β-strand312-31989
α-helix323-33614
β-strand341110
β-strand349-35469
β-strand363-37089
α-helix374-39017
α-helix396-3994
α-helix407-41913
α-helix422-4243
Chain K: 11 helices, 15 β-strands
ElementResiduesLengthSheet
β-strand107-11151
α-helix117-1237
β-strand14112
β-strand14912
β-strand158-15921
α-helix165-1684
α-helix169-1735
α-helix174-1818
β-strand186-19161
α-helix198-2025
α-helix219-23113
β-strand240-24781
β-strand252-25431
β-strand26813
β-strand27813
β-strand285-28731
α-helix290-2923
α-helix293-30210
β-strand319-32681
β-strand32814
β-strand35214
β-strand356-35941
α-helix374-39522
α-helix410-4145
β-strand424-42961
α-helix446-4505

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Kinesin-like protein cut7Kprotein438Schizosaccharomyces pombeP24339 (AlphaFold model)
Tubulin beta chainBprotein448Schizosaccharomyces pombeP05219 (AlphaFold model)
Tubulin alpha-1 chainAprotein455Schizosaccharomyces pombeP04688 (AlphaFold model)
Sequence of entity 1 (K), FASTA
>6S8M_1 Kinesin-like protein cut7 (chains K)
GIDPFTMAPRVAPGGSQQFLGKQGLKAKNPVSTPNSHFRSASNPRKRREPPTIDTGYPDR
SDTNSPTDHALHDENETNINVVVRVRGRTDQEVRDNSSLAVSTSGAMGAELAIQSDPSSM
LVTKTYAFDKVFGPEADQLMLFENSVAPMLEQVLNGYNCTIFAYGQTGTGKTYTMSGDLS
DSDGILSEGAGLIPRALYQLFSSLDNSNQEYAVKCSYYELYNEEIRDLLVSEELRKPARV
FEDTSRRGNVVITGIEESYIKNAGDGLRLLREGSHRRQVAATKCNDLSSRSHSIFTITLH
RKVSSGMTDETNSLTINNNSDDLLRASKLHMVDLAGSENIGRSGAENKRARETGMINQSL
LTLGRVINALVEKAHHIPYRESKLTRLLQDSLGGKTKTSMIVTVSSTNTNLEETISTLEY
AARAKSIRNKPQNNQLVF
Sequence of entity 2 (B), FASTA
>6S8M_2 Tubulin beta chain (chains B)
MREIVHIQAGQCGNQVGAAFWSTIADEHGLDSAGIYHGTSEAQHERLNVYFNEAAGGKYV
PRAVLVDLEPGTMDAVKSGKFGNLFRPDNIIYGQSGAGNIWAKGHYTEGAELADAVLDVV
RREAEACDALQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRMMATFSVAPAPKSSDTVV
EPYNATLSMHQLVENSDETFCIDNEALSSIFANTLKIKSPSYDDLNHLVSAVMAGVTTSF
RFPGELNSDLRKLAVNMVPFPRLHFFMVGFAPLAAIGSSSFQAVSVPELTQQMFDANNMM
VAADPRHGRYLTVAALFRGKVSMKEVDEQIRSVQTKNSAYFVEWIPDNVLKAVCSVPPKD
LKMSATFIGNSTSIQEIFRRLGDQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQEAGIDEGDEDYEIEEEKEPLEY
Sequence of entity 3 (A), FASTA
>6S8M_3 Tubulin alpha-1 chain (chains A)
MREVISVHVGQAGVQIGNACWELYCLEHGIGPDGFPTENSEVHKNNSYLNDGFGTFFSET
GQGKFVPRSIYVDLEPNVIDQVRTGPYKDLFHPEQMVTGKEDASNNYARGHYTVGKEMID
SVLERIRRMADNCSGLQGFLVFHSFGGGTGSGLGALLLERLNMEYGKKSNLQFSVYPAPQ
VSTSVVEPYNSVLTTHATLDNSDCTFMVDNEACYDICRRNLDIERPTYENLNRLIAQVVS
SITASLRFAGSLNVDLNEFQTNLVPYPRIHFPLVTYSPIVSAAKAFHESNSVQEITNQCF
EPYNQMVKCDPRTGRYMATCLLYRGDVIPRDVQAAVTSIKSRRTIQFVDWCPTGFKIGIC
YEPPQHVPGSGIAKVNRAVCMLSNTTSIAEAWSRLDHKFDLMYSKRAFVHWYVGEGMEEG
EFSEAREDLAALERDYEEVGQDSMDNEMYEADEEY

Ligands and cofactors

IDNameFormulaCopies
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P31
EPB7,11-dihydroxy-8,8,10,12,16-pentamethyl-3-[1-methyl-2-(2-methyl-thiazol-4-yl)vi…C27 H41 N O6 S1
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31
MGMagnesium ionMg1

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 6S8M 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.