5HNZ: Tubulin alpha-1B chain

Structural basis of backwards motion in kinesin-14: plus-end directed nKn669 in the nucleotide-free state. Determined by electron microscopy at 5.8 Å resolution. Released 10 Aug 2016.

Method
Electron microscopy
Resolution
5.8 Å
Organisms
Bos taurus, Drosophila melanogaster, Rattus norvegicus
Chains
3
Atoms
9,177
Mol. weight
143.58 kDa
Ligands
GDP, TA1, GTP, MG
Released
10 Aug 2016

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

Secondary structure: helices and β-sheets

5HNZ contains 54 α-helices and 52 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: 14 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand25-3177
α-helix32-354
α-helix36-394
β-strand48-5038
β-strand54-5638
β-strand5719
β-strand6019
β-strand6318
β-strand66-6837
α-helix74-785
α-helix79-835
α-helix84-907
β-strand95-10067
α-helix107-1115
β-strand113110
β-strand121110
α-helix124-13411
β-strand142-154137
β-strand157-16047
β-strand16917
β-strand170-173411
β-strand179-182411
β-strand187-18827
α-helix192-20312
β-strand208112
β-strand218112
β-strand221-232127
β-strand238-248117
α-helix249-2513
α-helix261-28525
α-helix293-2953
α-helix297-3015
α-helix303-3064
β-strand311-31887
α-helix325-33814

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tubulin alpha-1B chainAprotein451Bos taurusP81947 (AlphaFold model)
Tubulin beta-2B chainBprotein445Bos taurusQ6B856 (AlphaFold model)
Protein claret segregational,Protein claret segregational,Plus-end directed…Kprotein371Drosophila melanogaster, Rattus norvegicusP20480 (AlphaFold model), P56536 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5HNZ_1 Tubulin alpha-1B chain (chains A)
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGK
HVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD
RIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTA
VVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITA
SLRFDGALNVDLTEFQTNLVPYPRGHFPLATYAPVISAEKAYHEQLSVAEITNACFEPAN
QMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPP
TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSE
AREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Sequence of entity 2 (B), FASTA
>5HNZ_2 Tubulin beta-2B chain (chains B)
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYV
PRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV
RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVV
EPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL
RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMM
AACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG
LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVS
EYQQYQDATADEQGEFEEEEGEDEA
Sequence of entity 3 (K), FASTA
>5HNZ_3 Protein claret segregational,Protein claret segregational,Plus-end directed kinesin-1/kinesin-14,Protein claret segregational,Protein claret segregational (chains K)
KEQLFQSNMERKELHNTVMDLRGNIKVMCRFRPLNEAEILRGDKFIPKFKGEETVVIQGK
PYVFDRVLPPNTTQEQVYNACAKQIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPQL
MGIIPRIAHDIFDHIYSMDENLEFAIKVSYFEIYLDKIRDLLDVSKTNLAVHEDKNRVPY
VKGCTERFVSSPEEVMDVIDEGKSNRHVAVTNMNEHSSRSHSIFLINIKQENVETEKKLS
GKLYLVDLAGSEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGTTHVPYRDSKMTR
ILQDSLGGNCRTTIVICCSPSVFNEAETKSTLMFGQRAKSCKMTKAKRNRYLNNSVANSS
TQSNNSGSFDK

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21
TA1TaxolC47 H51 N O141
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P31
MGMagnesium ionMg1

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:

Browse structure collections

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