Human Kinesin Motor Domain With Docked Neck Linker. Determined by X-ray diffraction at 2.7 Å resolution. Released 30 Oct 2002.
Explore 1MKJ in 3D Show helices and sheets RCSB PDB PDBe
1MKJ contains 16 α-helices and 25 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-8 | 4 | 1 |
| α-helix | 9 | 1 | |
| β-strand | 10-15 | 6 | 2 |
| α-helix | 17-19 | 3 | |
| α-helix | 20-24 | 5 | |
| β-strand | 29 | 1 | 3 |
| β-strand | 32-34 | 3 | 4 |
| β-strand | 38-40 | 3 | 4 |
| β-strand | 45-47 | 3 | 4 |
| β-strand | 50-52 | 3 | 2 |
| α-helix | 58-74 | 17 | |
| β-strand | 79-84 | 6 | 2 |
| α-helix | 91-95 | 5 | |
| β-strand | 97 | 1 | 5 |
| β-strand | 105 | 1 | 5 |
| α-helix | 107-119 | 13 | |
| β-strand | 126-138 | 13 | 2 |
| β-strand | 141-144 | 4 | 2 |
| β-strand | 147 | 1 | 2 |
| β-strand | 153 | 1 | 2 |
| β-strand | 154-157 | 4 | 6 |
| β-strand | 163-166 | 4 | 6 |
| β-strand | 171-173 | 3 | 2 |
| α-helix | 176-189 | 14 | |
| α-helix | 197-203 | 7 | |
| β-strand | 205-216 | 12 | 2 |
| β-strand | 221-231 | 11 | 2 |
| α-helix | 232-234 | 3 | |
| β-strand | 237 | 1 | 7 |
| β-strand | 253 | 1 | 7 |
| α-helix | 256-270 | 15 | |
| α-helix | 277-279 | 3 | |
| α-helix | 281-285 | 5 | |
| α-helix | 287-290 | 4 | |
| β-strand | 295-302 | 8 | 2 |
| β-strand | 305 | 1 | 3 |
| α-helix | 306-308 | 3 | |
| α-helix | 309-323 | 15 | |
| β-strand | 326-329 | 4 | 1 |
| β-strand | 333-334 | 2 | 2 |
| α-helix | 337-348 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinesin heavy chain | A | protein | 349 | Homo sapiens | P33176 (AlphaFold model) |
>1MKJ_1 KINESIN HEAVY CHAIN (chains A) MADLAECNIKVMCRFRPLNESEVNRGDKYIAKFQGEDTVVIASKPYAFDRVFQSSTSQEQ VYNDCAKKIVKDVLEGYNGTIFAYGQTSSGKTHTMEGKLHDPEGMGIIPRIVQDIFNYIY SMDENLEFHIKVSYFEIYLDKIRDLLDVSKTNLSVHEDKNRVPYVKGCTERFVCSPDEVM DTIDEGKSNRHVAVTNMNEHSSRSHSIFLINVKQENTQTEQKLSGKLYLVDLAGSEKVSK TGAEGAVLDEAKNINKSLSALGNVISALAEGSTYVPYRDSKMTRILQDSLGGNCRTTIVI CCSPSSYNESETKSTLLFGQRAKTIKNTVCVNVELTAEQWKKKYEKEKE
Water and common crystallization additives (SO4) are not listed.
Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy. Sindelar, C.V., Budny, M.J., Rice, S. et al. Nat Struct Biol (2002) 9:844-848. 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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