9L78: Nucleotide-free human kinesin-1 motor domain

Crystal structure of nucleotide-free human kinesin-1 motor domain (G234A mutant). Determined by X-ray diffraction at 2.82 Å resolution. Released 23 Apr 2025.

Method
X-ray diffraction
Resolution
2.82 Å
Organism
Homo sapiens
Chains
2
Atoms
4,762
Mol. weight
76.61 kDa
Released
23 Apr 2025

Explore 9L78 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9L78 contains 25 α-helices and 35 β-strands across 2 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: 14 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand9-1571
α-helix17-193
α-helix20-256
β-strand31-3442
β-strand38-4142
β-strand44-4742
β-strand50-5231
α-helix58-658
α-helix67-737
β-strand79-8571
α-helix91-955
β-strand9713
β-strand10513
α-helix107-11913
β-strand126-138131
β-strand141-14441
β-strand154-15744
β-strand163-16644
β-strand171-17221
α-helix176-18813
β-strand205-216121
β-strand221-231111
α-helix232-2343
α-helix247-27024
α-helix277-2793
α-helix282-2854
α-helix287-2904
β-strand295-30281
α-helix306-3083
α-helix309-32214
Chain B: 11 helices, 19 β-strands
ElementResiduesLengthSheet
β-strand9-1575
β-strand2916
β-strand32-3437
β-strand38-4147
β-strand44-4747
β-strand50-5235
α-helix58-658
α-helix67-737
β-strand79-8465
α-helix91-955
β-strand9718
β-strand10518
α-helix107-12014
β-strand126-138135
β-strand141-14445
β-strand15115
β-strand154-15749
β-strand163-16649
β-strand171-17335
α-helix176-18813
β-strand205-216125
β-strand222-231105
α-helix232-2343
α-helix247-26923
α-helix277-2793
α-helix282-2854
α-helix287-2904
β-strand295-30285
β-strand30516
α-helix309-32012

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Kinesin-1 heavy chainA, Bprotein342Homo sapiensP33176 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9L78_1 Kinesin-1 heavy chain (chains A, B)
MHHHHHHADLAESNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQS
STSQEQVYNDAAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQD
IFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGATERFVS
SPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAA
SEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNA
RTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVSVNVELT

Primary citation

Tension-induced suppression of allosteric conformational changes coordinates kinesin-1 stepping. Makino, T., Kanada, R., Mori, T. et al. J Cell Biol (2025) 224. DOI 10.1083/jcb.202501253 · PubMed

Other PDB entries of the same protein (UniProt P33176 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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