5HNW: Tubulin alpha-1B chain

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.

Method
Electron microscopy
Resolution
6.6 Å
Organisms
Bos taurus, Drosophila melanogaster, Rattus norvegicus
Chains
3
Atoms
9,302
Mol. weight
143.75 kDa
Ligands
GDP, TA1, ANP, GTP
Released
10 Aug 2016

Explore 5HNW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 19 helices, 14 β-strands

ElementResiduesLengthSheet
β-strand4-961
α-helix10-2617
β-strand65-6951
α-helix72-809
β-strand92-9431
α-helix103-1075
α-helix109-12820
β-strand134-13961
α-helix144-1496
α-helix150-16011
β-strand16511
β-strand167-17041
α-helix184-19411
β-strand200-20341
α-helix206-21510
α-helix224-24219
α-helix252-2598
β-strand269-27131
β-strand27712
α-helix288-2914
α-helix293-2964
β-strand312-321101
α-helix325-33612
β-strand34311
β-strand351-35551
β-strand36812
β-strand373-38191
α-helix382-3843
α-helix385-39915
α-helix403-4053
α-helix406-4094
α-helix415-42915
α-helix431-4344
Chain B: 21 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand413
β-strand6-943
α-helix12-2615
β-strand3014
β-strand3614
α-helix49-524
β-strand5515
β-strand6115
β-strand65-6953
α-helix72-787
α-helix83-853
α-helix89-913
β-strand92-9433
α-helix105-1095
α-helix111-12616
β-strand134-13963
α-helix144-1485
α-helix149-16012
β-strand165-17063
α-helix184-19411
β-strand200-20233
α-helix206-2149
α-helix224-24219
β-strand24816
α-helix252-2598
β-strand267-26823
β-strand269-27136
α-helix289-2957
α-helix307-3093
β-strand312-32096
α-helix325-33814
β-strand351-35666
β-strand375-38176
α-helix382-3843
α-helix385-39915
α-helix403-4053
α-helix406-4094
α-helix415-43622
Chain K: 13 helices, 15 β-strands
ElementResiduesLengthSheet
α-helix17-215
β-strand29-3137
α-helix32-354
α-helix36-394
β-strand48-5038
β-strand54-5638
β-strand67-6827
α-helix74-818
α-helix83-908
β-strand95-10067
α-helix107-1115
α-helix124-13411
β-strand142-154137
β-strand157-16047
β-strand171-17339
β-strand179-18139
β-strand186-18947
α-helix192-20312
β-strand208-209210
β-strand217-218210
β-strand221-232127
β-strand239-24797
α-helix248-2503
α-helix254-2574
α-helix265-28723
α-helix297-3015
β-strand312-31877
α-helix325-3339

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tubulin alpha-1B chainAprotein450Bos taurusP81947 (AlphaFold model)
Tubulin beta-2B chainBprotein444Bos taurusQ6B856 (AlphaFold model)
Protein claret segregational,KINESIN HEAVY CHAIN ISOFORM 5CKprotein371Drosophila melanogaster, Rattus norvegicusP20480 (AlphaFold model), P56536 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5HNW_1 Tubulin alpha-1B chain (chains A)
RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKH
VPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDR
IRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAV
VEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITAS
LRFDGALNVDLTEFQTNLVPYPRGHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQ
MVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPPT
VVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEA
REDMAALEKDYEEVGVDSVEGEGEEEGEEY
Sequence of entity 2 (B), FASTA
>5HNW_2 Tubulin beta-2B chain (chains B)
REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVP
RAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR
KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVE
PYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR
FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMA
ACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGL
KMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSE
YQQYQDATADEQGEFEEEEGEDEA
Sequence of entity 3 (K), FASTA
>5HNW_3 Protein claret segregational,KINESIN HEAVY CHAIN ISOFORM 5C (chains K)
KEQLFQSNMERKELHNTVMDLRGNIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIQGK
PYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQL
MGIIPRIAHDIFDHIYSMDENLEFAIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPY
VKGCTERFVSSPEEVMDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLS
GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTTHVPYRDSKMTR
ILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFAASVNSCKMTKAKRNRYLNNSVANSS
TQSNNSGSFDK

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21
TA1TaxolC47 H51 N O141
ANPPhosphoaminophosphonic acid-adenylate esterC10 H17 N6 O12 P31
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P31
MGMagnesium ionMg2

Primary citation

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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