9L6K: Nucleotide-free human kinesin-1 motor domain

Crystal structure of nucleotide-free human kinesin-1 motor domain (G234V mutant). Determined by X-ray diffraction at 2.8 Å resolution. Released 23 Apr 2025.

Method
X-ray diffraction
Resolution
2.8 Å
Organism
Homo sapiens
Chains
2
Atoms
5,015
Mol. weight
76.67 kDa
Released
23 Apr 2025

Explore 9L6K in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9L6K contains 27 α-helices and 36 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: 15 helices, 19 β-strands

ElementResiduesLengthSheet
β-strand9-1571
α-helix16-194
α-helix20-245
β-strand2912
β-strand31-3443
β-strand38-4143
β-strand44-4743
β-strand50-5231
α-helix58-658
α-helix67-737
β-strand79-8461
α-helix87-893
α-helix91-955
β-strand9714
β-strand10514
α-helix107-12115
β-strand126-138131
β-strand141-14441
β-strand155-15735
β-strand163-16535
β-strand171-17331
α-helix176-18712
β-strand205-216121
β-strand221-231111
α-helix236-2394
α-helix247-26923
α-helix277-2793
α-helix281-2855
α-helix287-2904
β-strand295-30281
β-strand30512
α-helix306-3083
α-helix309-32012
β-strand330-33236
Chain B: 12 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand9-1577
α-helix16-183
β-strand32-3438
β-strand38-4148
β-strand44-4748
β-strand50-5237
α-helix58-625
α-helix63-675
α-helix68-736
β-strand79-8467
α-helix87-893
α-helix91-955
β-strand9719
β-strand10519
α-helix107-12014
β-strand126-138137
β-strand141-14447
β-strand155110
β-strand165110
β-strand171-17337
α-helix176-18712
β-strand205-216127
β-strand221-231117
α-helix247-26923
α-helix277-2793
α-helix281-2855
β-strand296-30277
α-helix311-32212
β-strand328-33036

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Kinesin-1 heavy chainA, Bprotein342Homo sapiensP33176 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9L6K_1 Kinesin-1 heavy chain (chains A, B)
MHHHHHHADLAESNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQS
STSQEQVYNDAAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQD
IFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGATERFVS
SPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAV
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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