9L7E: Human kinesin-1 motor domain

Crystal structure of human kinesin-1 motor domain (G234A mutant) in complex with ADP. Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Apr 2025.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,445
Mol. weight: 40.47 kDa
Ligands: ADP, MG
Released: 23 Apr 2025

Explore 9L7E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9L7E contains 14 α-helices and 19 β-strands across 1 chain. 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, 19 β-strands

Element	Residues	Length	Sheet
β-strand	9-15	7	1
α-helix	16-19	4
α-helix	20-24	5
β-strand	29	1	2
β-strand	32-34	3	3
β-strand	38-41	4	3
β-strand	44-47	4	3
β-strand	50-52	3	1
α-helix	58-65	8
α-helix	67-74	8
β-strand	79-85	7	1
α-helix	91-95	5
β-strand	97	1	4
β-strand	105	1	4
α-helix	107-120	14
β-strand	126-138	13	1
β-strand	141-144	4	1
β-strand	153	1	1
β-strand	155-156	2	5
β-strand	164-165	2	5
β-strand	171-172	2	1
α-helix	176-189	14
α-helix	197-202	6
β-strand	205-216	12	1
β-strand	222-231	10	1
α-helix	232-234	3
α-helix	256-269	14
α-helix	277-279	3
α-helix	281-285	5
β-strand	295-302	8	1
β-strand	305	1	2
α-helix	306-308	3
α-helix	309-320	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Kinesin-1 heavy chain	A	protein	355	Homo sapiens	P33176 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9L7E_1 Kinesin-1 heavy chain (chains A)
MADLAESNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQ
VYNDAAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIY
SMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGATERFVSSPDEVM
DTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAASEKVSK
TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNARTTIVI
CCSPSSYNESETKSTLLFGQRAKTIKNTVSVNVELTAEQWKKKYEKEKEHHHHHH

Ligands and cofactors

ID	Name	Formula	Copies
ADP	Adenosine-5'-diphosphate	C10 H15 N5 O10 P2	1
MG	Magnesium ion	Mg	1

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:

1BG2 1.8 Å, Human ubiquitous kinesin motor domain
5LT1 1.95 Å, nucleotide-free kinesin-1 motor domain T92V mutant, P21 crystal form
5LT0 2.0 Å, nucleotide-free kinesin-1 motor domain, P212121 crystal form
4LNU 2.19 Å, Nucleotide-free kinesin motor domain in complex with tubulin and a DARPin
5LT3 2.59 Å, nucleotide-free kinesin-1 motor domain T87A mutant, P1 crystal form
5LT2 2.6 Å, nucleotide-free kinesin-1 motor domain, P1 crystal form
1MKJ 2.7 Å, Human Kinesin Motor Domain With Docked Neck Linker
9L6K 2.8 Å, Crystal structure of nucleotide-free human kinesin-1 motor domain (G234V mutant)
9L78 2.82 Å, Crystal structure of nucleotide-free human kinesin-1 motor domain (G234A mutant)
5LT4 2.88 Å, nucleotide-free kinesin-1 motor domain T92V mutant, P1 crystal form
9GNQ 2.9 Å, Microtubule-associated Kif5B IAK tail mutant bound to ADP
7TR2 3.0 Å, Apo CaKip3[2-436]-L2-mutant(HsKHC) in complex with a microtubule

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