Molecular basis of human kinesin-8 function and inhibition. Determined by electron microscopy at 4.8 Å resolution. Released 25 Oct 2017.
Explore 5OGC in 3D Show helices and sheets RCSB PDB PDBe
5OGC contains 59 α-helices and 45 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 | 4-9 | 6 | 5 |
| α-helix | 10-28 | 19 | |
| β-strand | 65-69 | 5 | 5 |
| α-helix | 72-80 | 9 | |
| β-strand | 92-94 | 3 | 5 |
| α-helix | 103-107 | 5 | |
| α-helix | 111-128 | 18 | |
| β-strand | 134-139 | 6 | 5 |
| α-helix | 145-149 | 5 | |
| α-helix | 150-160 | 11 | |
| β-strand | 165-170 | 6 | 5 |
| α-helix | 183-195 | 13 | |
| β-strand | 202-203 | 2 | 5 |
| α-helix | 206-215 | 10 | |
| α-helix | 224-238 | 15 | |
| β-strand | 248 | 1 | 5 |
| α-helix | 252-259 | 8 | |
| β-strand | 269-270 | 2 | 5 |
| β-strand | 277 | 1 | 6 |
| α-helix | 288-291 | 4 | |
| α-helix | 293-295 | 3 | |
| α-helix | 298-300 | 3 | |
| β-strand | 312-321 | 10 | 5 |
| α-helix | 325-336 | 12 | |
| β-strand | 351-355 | 5 | 5 |
| α-helix | 359-360 | 2 | |
| β-strand | 368 | 1 | 6 |
| β-strand | 373-381 | 9 | 5 |
| α-helix | 384-399 | 16 | |
| α-helix | 403-405 | 3 | |
| α-helix | 406-409 | 4 | |
| α-helix | 415-434 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-9 | 7 | 7 |
| α-helix | 10-26 | 17 | |
| β-strand | 30 | 1 | 8 |
| β-strand | 36 | 1 | 8 |
| α-helix | 49-52 | 4 | |
| β-strand | 53-55 | 3 | 9 |
| β-strand | 61-63 | 3 | 9 |
| β-strand | 65-69 | 5 | 7 |
| α-helix | 72-78 | 7 | |
| α-helix | 83-85 | 3 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 7 |
| α-helix | 103-104 | 2 | |
| α-helix | 105-109 | 5 | |
| α-helix | 110-126 | 17 | |
| β-strand | 132-140 | 9 | 7 |
| α-helix | 144-149 | 6 | |
| α-helix | 150-160 | 11 | |
| β-strand | 165-171 | 7 | 7 |
| α-helix | 172-174 | 3 | |
| α-helix | 184-194 | 11 | |
| β-strand | 200-203 | 4 | 7 |
| α-helix | 206-211 | 6 | |
| α-helix | 212-216 | 5 | |
| α-helix | 224-242 | 19 | |
| β-strand | 248 | 1 | 10 |
| α-helix | 252-259 | 8 | |
| β-strand | 267-268 | 2 | 7 |
| β-strand | 269-271 | 3 | 10 |
| α-helix | 289-295 | 7 | |
| α-helix | 307-309 | 3 | |
| β-strand | 312-320 | 9 | 10 |
| α-helix | 327-338 | 12 | |
| α-helix | 340-342 | 3 | |
| β-strand | 351-356 | 6 | 10 |
| β-strand | 374-381 | 8 | 10 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 406-409 | 4 | |
| α-helix | 415-436 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-18 | 7 | 1 |
| α-helix | 23-28 | 6 | |
| β-strand | 34-36 | 3 | 2 |
| β-strand | 41-44 | 4 | 2 |
| β-strand | 72-75 | 4 | 2 |
| β-strand | 78-80 | 3 | 1 |
| α-helix | 86-89 | 4 | |
| α-helix | 90-94 | 5 | |
| α-helix | 95-103 | 9 | |
| β-strand | 107-111 | 5 | 1 |
| α-helix | 119-123 | 5 | |
| α-helix | 132-150 | 19 | |
| β-strand | 153-163 | 11 | 1 |
| β-strand | 166-169 | 4 | 1 |
| α-helix | 177-178 | 2 | |
| β-strand | 179-181 | 3 | 3 |
| β-strand | 187-189 | 3 | 3 |
| β-strand | 195 | 1 | 1 |
| α-helix | 200-213 | 14 | |
| α-helix | 215-216 | 2 | |
| β-strand | 217 | 1 | 4 |
| β-strand | 223 | 1 | 4 |
| β-strand | 229-238 | 10 | 1 |
| α-helix | 248-249 | 2 | |
| β-strand | 250-258 | 9 | 1 |
| α-helix | 260-263 | 4 | |
| α-helix | 265-268 | 4 | |
| α-helix | 272-300 | 29 | |
| α-helix | 307-309 | 3 | |
| α-helix | 311-320 | 10 | |
| β-strand | 326-332 | 7 | 1 |
| α-helix | 338-354 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinesin-like protein KIF18A | K | protein | 377 | Homo sapiens | Q8NI77 (AlphaFold model) |
| Tubulin alpha chain | A | protein | 451 | Bos taurus | P81947 (AlphaFold model) |
| Tubulin beta chain | B | protein | 445 | Sus scrofa | P02554 (AlphaFold model) |
>5OGC_1 Kinesin-like protein KIF18A (chains K) GSHMSVTEEDLCHHMKVVVRVRPENTKEKAAGFHKVVHVVDKHILVFDPKQEEVSFFHGK KTTNQNVIKKQNKDLKFVFDAVFDETSTQSEVFEHTTKPILRSFLNGYNCTVLAYGATGA GKTHTMLGSADEPGVMYLTMLHLYKCMDEIKEEKICSTAVSYLEVYNEQIRDLLVNSGPL AVREDTQKGVVVHGLTLHQPKSSEEILHLLDNGNKNRTQHPTDMNATSSRSHAVFQIYLR QQDKTASINQNVRIAKMSLIDLAGSERASTSGAKGTRFVEGTNINRSLLALGNVINALAD SKRKNQHIPYRNSKLTRLLKDSLGGNCQTIMIAAVSPSSVFYDDTYNTLKYANRAKDIKS SLKSNVLNVNNHITQYV
>5OGC_2 Tubulin alpha chain (chains A) MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRGHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE AREDMAALEKDYEEVGVDSVEGEGEEEGEEY
>5OGC_3 Tubulin beta chain (chains B) MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS EYQQYQDATADEQGEFEEEGEEDEA
| ID | Name | Formula | Copies |
|---|---|---|---|
| TA1 | Taxol | C47 H51 N O14 | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 1 |
| MG | Magnesium ion | Mg | 1 |
| ZN | Zinc ion | Zn | 1 |
| 9V5 | 4-chloranyl-2-nitro-1-(phenylsulfonyl)benzene | C12 H8 Cl N O4 S | 1 |
Structural basis of human kinesin-8 function and inhibition. Locke, J., Joseph, A.P., Pena, A. et al. Proc Natl Acad Sci U S A (2017) 114:E9539-E9548. DOI 10.1073/pnas.1712169114 · PubMed
Other PDB entries of the same protein (UniProt Q8NI77 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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