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.
Explore 9L78 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-15 | 7 | 1 |
| α-helix | 17-19 | 3 | |
| α-helix | 20-25 | 6 | |
| β-strand | 31-34 | 4 | 2 |
| β-strand | 38-41 | 4 | 2 |
| β-strand | 44-47 | 4 | 2 |
| β-strand | 50-52 | 3 | 1 |
| α-helix | 58-65 | 8 | |
| α-helix | 67-73 | 7 | |
| β-strand | 79-85 | 7 | 1 |
| α-helix | 91-95 | 5 | |
| β-strand | 97 | 1 | 3 |
| β-strand | 105 | 1 | 3 |
| α-helix | 107-119 | 13 | |
| β-strand | 126-138 | 13 | 1 |
| β-strand | 141-144 | 4 | 1 |
| β-strand | 154-157 | 4 | 4 |
| β-strand | 163-166 | 4 | 4 |
| β-strand | 171-172 | 2 | 1 |
| α-helix | 176-188 | 13 | |
| β-strand | 205-216 | 12 | 1 |
| β-strand | 221-231 | 11 | 1 |
| α-helix | 232-234 | 3 | |
| α-helix | 247-270 | 24 | |
| α-helix | 277-279 | 3 | |
| α-helix | 282-285 | 4 | |
| α-helix | 287-290 | 4 | |
| β-strand | 295-302 | 8 | 1 |
| α-helix | 306-308 | 3 | |
| α-helix | 309-322 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-15 | 7 | 5 |
| β-strand | 29 | 1 | 6 |
| β-strand | 32-34 | 3 | 7 |
| β-strand | 38-41 | 4 | 7 |
| β-strand | 44-47 | 4 | 7 |
| β-strand | 50-52 | 3 | 5 |
| α-helix | 58-65 | 8 | |
| α-helix | 67-73 | 7 | |
| β-strand | 79-84 | 6 | 5 |
| α-helix | 91-95 | 5 | |
| β-strand | 97 | 1 | 8 |
| β-strand | 105 | 1 | 8 |
| α-helix | 107-120 | 14 | |
| β-strand | 126-138 | 13 | 5 |
| β-strand | 141-144 | 4 | 5 |
| β-strand | 151 | 1 | 5 |
| β-strand | 154-157 | 4 | 9 |
| β-strand | 163-166 | 4 | 9 |
| β-strand | 171-173 | 3 | 5 |
| α-helix | 176-188 | 13 | |
| β-strand | 205-216 | 12 | 5 |
| β-strand | 222-231 | 10 | 5 |
| α-helix | 232-234 | 3 | |
| α-helix | 247-269 | 23 | |
| α-helix | 277-279 | 3 | |
| α-helix | 282-285 | 4 | |
| α-helix | 287-290 | 4 | |
| β-strand | 295-302 | 8 | 5 |
| β-strand | 305 | 1 | 6 |
| α-helix | 309-320 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinesin-1 heavy chain | A, B | protein | 342 | Homo sapiens | P33176 (AlphaFold model) |
>9L78_1 Kinesin-1 heavy chain (chains A, B) MHHHHHHADLAESNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQS STSQEQVYNDAAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQD IFNYIYSMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGATERFVS SPDEVMDTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAA SEKVSKTGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNA RTTIVICCSPSSYNESETKSTLLFGQRAKTIKNTVSVNVELT
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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