Structural basis of backwards motion in kinesin-14: minus-end directed nKn664 in the AMPPNP state. Determined by electron microscopy at 6.6 Å resolution. Released 10 Aug 2016.
Explore 5HNW in 3D Show helices and sheets RCSB PDB PDBe
5HNW contains 53 α-helices and 46 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 | 1 |
| α-helix | 10-26 | 17 | |
| β-strand | 65-69 | 5 | 1 |
| α-helix | 72-80 | 9 | |
| β-strand | 92-94 | 3 | 1 |
| α-helix | 103-107 | 5 | |
| α-helix | 109-128 | 20 | |
| β-strand | 134-139 | 6 | 1 |
| α-helix | 144-149 | 6 | |
| α-helix | 150-160 | 11 | |
| β-strand | 165 | 1 | 1 |
| β-strand | 167-170 | 4 | 1 |
| α-helix | 184-194 | 11 | |
| β-strand | 200-203 | 4 | 1 |
| α-helix | 206-215 | 10 | |
| α-helix | 224-242 | 19 | |
| α-helix | 252-259 | 8 | |
| β-strand | 269-271 | 3 | 1 |
| β-strand | 277 | 1 | 2 |
| α-helix | 288-291 | 4 | |
| α-helix | 293-296 | 4 | |
| β-strand | 312-321 | 10 | 1 |
| α-helix | 325-336 | 12 | |
| β-strand | 343 | 1 | 1 |
| β-strand | 351-355 | 5 | 1 |
| β-strand | 368 | 1 | 2 |
| β-strand | 373-381 | 9 | 1 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 403-405 | 3 | |
| α-helix | 406-409 | 4 | |
| α-helix | 415-429 | 15 | |
| α-helix | 431-434 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4 | 1 | 3 |
| β-strand | 6-9 | 4 | 3 |
| α-helix | 12-26 | 15 | |
| β-strand | 30 | 1 | 4 |
| β-strand | 36 | 1 | 4 |
| α-helix | 49-52 | 4 | |
| β-strand | 55 | 1 | 5 |
| β-strand | 61 | 1 | 5 |
| β-strand | 65-69 | 5 | 3 |
| α-helix | 72-78 | 7 | |
| α-helix | 83-85 | 3 | |
| α-helix | 89-91 | 3 | |
| β-strand | 92-94 | 3 | 3 |
| α-helix | 105-109 | 5 | |
| α-helix | 111-126 | 16 | |
| β-strand | 134-139 | 6 | 3 |
| α-helix | 144-148 | 5 | |
| α-helix | 149-160 | 12 | |
| β-strand | 165-170 | 6 | 3 |
| α-helix | 184-194 | 11 | |
| β-strand | 200-202 | 3 | 3 |
| α-helix | 206-214 | 9 | |
| α-helix | 224-242 | 19 | |
| β-strand | 248 | 1 | 6 |
| α-helix | 252-259 | 8 | |
| β-strand | 267-268 | 2 | 3 |
| β-strand | 269-271 | 3 | 6 |
| α-helix | 289-295 | 7 | |
| α-helix | 307-309 | 3 | |
| β-strand | 312-320 | 9 | 6 |
| α-helix | 325-338 | 14 | |
| β-strand | 351-356 | 6 | 6 |
| β-strand | 375-381 | 7 | 6 |
| α-helix | 382-384 | 3 | |
| α-helix | 385-399 | 15 | |
| α-helix | 403-405 | 3 | |
| α-helix | 406-409 | 4 | |
| α-helix | 415-436 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-21 | 5 | |
| β-strand | 29-31 | 3 | 7 |
| α-helix | 32-35 | 4 | |
| α-helix | 36-39 | 4 | |
| β-strand | 48-50 | 3 | 8 |
| β-strand | 54-56 | 3 | 8 |
| β-strand | 67-68 | 2 | 7 |
| α-helix | 74-81 | 8 | |
| α-helix | 83-90 | 8 | |
| β-strand | 95-100 | 6 | 7 |
| α-helix | 107-111 | 5 | |
| α-helix | 124-134 | 11 | |
| β-strand | 142-154 | 13 | 7 |
| β-strand | 157-160 | 4 | 7 |
| β-strand | 171-173 | 3 | 9 |
| β-strand | 179-181 | 3 | 9 |
| β-strand | 186-189 | 4 | 7 |
| α-helix | 192-203 | 12 | |
| β-strand | 208-209 | 2 | 10 |
| β-strand | 217-218 | 2 | 10 |
| β-strand | 221-232 | 12 | 7 |
| β-strand | 239-247 | 9 | 7 |
| α-helix | 248-250 | 3 | |
| α-helix | 254-257 | 4 | |
| α-helix | 265-287 | 23 | |
| α-helix | 297-301 | 5 | |
| β-strand | 312-318 | 7 | 7 |
| α-helix | 325-333 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tubulin alpha-1B chain | A | protein | 450 | Bos taurus | P81947 (AlphaFold model) |
| Tubulin beta-2B chain | B | protein | 444 | Bos taurus | Q6B856 (AlphaFold model) |
| Protein claret segregational,KINESIN HEAVY CHAIN ISOFORM 5C | K | protein | 371 | Drosophila melanogaster, Rattus norvegicus | P20480 (AlphaFold model), P56536 (AlphaFold model) |
>5HNW_1 Tubulin alpha-1B chain (chains A) RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKH VPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDR IRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAV VEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITAS LRFDGALNVDLTEFQTNLVPYPRGHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQ MVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPPT VVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEA REDMAALEKDYEEVGVDSVEGEGEEEGEEY
>5HNW_2 Tubulin beta-2B chain (chains B) REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVP RAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVE PYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMA ACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGL KMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSE YQQYQDATADEQGEFEEEEGEDEA
>5HNW_3 Protein claret segregational,KINESIN HEAVY CHAIN ISOFORM 5C (chains K) KEQLFQSNMERKELHNTVMDLRGNIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIQGK PYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQL MGIIPRIAHDIFDHIYSMDENLEFAIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPY VKGCTERFVSSPEEVMDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLS GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTTHVPYRDSKMTR ILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFAASVNSCKMTKAKRNRYLNNSVANSS TQSNNSGSFDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 1 |
| TA1 | Taxol | C47 H51 N O14 | 1 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 1 |
| GTP | Guanosine-5'-triphosphate | C10 H16 N5 O14 P3 | 1 |
| MG | Magnesium ion | Mg | 2 |
Structural Basis of Backwards Motion in Kinesin-1-Kinesin-14 Chimera: Implication for Kinesin-14 Motility. Yamagishi, M., Shigematsu, H., Yokoyama, T. et al. Structure (2016) 24:1322-1334. DOI 10.1016/j.str.2016.05.021 · PubMed
Other PDB entries of the same protein (UniProt P81947 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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