Crystal Structure of the Mitotic Kinesin Eg5 in Complex with Mg-ADP. Determined by X-ray diffraction at 2.1 Å resolution. Released 18 Jul 2001.
Explore 1II6 in 3D Show helices and sheets RCSB PDB PDBe
1II6 contains 37 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 19-25 | 7 | 1 |
| α-helix | 30-34 | 5 | |
| β-strand | 39 | 1 | 2 |
| β-strand | 41-44 | 4 | 3 |
| β-strand | 49-53 | 5 | 3 |
| β-strand | 63-67 | 5 | 3 |
| β-strand | 70-72 | 3 | 1 |
| α-helix | 78-81 | 4 | |
| α-helix | 82-86 | 5 | |
| α-helix | 87-94 | 8 | |
| β-strand | 98-105 | 8 | 1 |
| α-helix | 111-115 | 5 | |
| β-strand | 117 | 1 | 4 |
| α-helix | 129-130 | 2 | |
| β-strand | 133 | 1 | 4 |
| α-helix | 135-149 | 15 | |
| β-strand | 153-164 | 12 | 1 |
| β-strand | 167-170 | 4 | 1 |
| β-strand | 183-185 | 3 | 5 |
| α-helix | 186-187 | 2 | |
| β-strand | 195-197 | 3 | 5 |
| β-strand | 202-204 | 3 | 1 |
| α-helix | 207-209 | 3 | |
| α-helix | 210-226 | 17 | |
| α-helix | 232-234 | 3 | |
| β-strand | 236-247 | 12 | 1 |
| β-strand | 255-265 | 11 | 1 |
| α-helix | 266-268 | 3 | |
| α-helix | 282-304 | 23 | |
| α-helix | 311-313 | 3 | |
| α-helix | 315-319 | 5 | |
| α-helix | 321-324 | 4 | |
| β-strand | 330-336 | 7 | 1 |
| β-strand | 339 | 1 | 2 |
| α-helix | 340-342 | 3 | |
| α-helix | 343-356 | 14 | |
| α-helix | 360-362 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 19-25 | 7 | 6 |
| α-helix | 26-28 | 3 | |
| α-helix | 30-34 | 5 | |
| α-helix | 37-38 | 2 | |
| β-strand | 39 | 1 | 7 |
| β-strand | 41-44 | 4 | 8 |
| β-strand | 49-53 | 5 | 8 |
| β-strand | 63-67 | 5 | 8 |
| β-strand | 70-72 | 3 | 6 |
| α-helix | 78-81 | 4 | |
| α-helix | 82-86 | 5 | |
| α-helix | 87-94 | 8 | |
| β-strand | 98-105 | 8 | 6 |
| α-helix | 111-115 | 5 | |
| β-strand | 117 | 1 | 9 |
| β-strand | 133 | 1 | 9 |
| α-helix | 135-149 | 15 | |
| β-strand | 153-164 | 12 | 6 |
| β-strand | 167-170 | 4 | 6 |
| β-strand | 184-187 | 4 | 10 |
| β-strand | 190-196 | 7 | 10 |
| β-strand | 202-204 | 3 | 6 |
| α-helix | 209-228 | 20 | |
| α-helix | 232-234 | 3 | |
| β-strand | 236-247 | 12 | 6 |
| β-strand | 255-265 | 11 | 6 |
| α-helix | 266-268 | 3 | |
| α-helix | 269-271 | 3 | |
| α-helix | 291-303 | 13 | |
| α-helix | 311-313 | 3 | |
| α-helix | 315-319 | 5 | |
| β-strand | 330-336 | 7 | 6 |
| β-strand | 339 | 1 | 7 |
| α-helix | 340-342 | 3 | |
| α-helix | 343-356 | 14 | |
| α-helix | 360-363 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinesin-related motor protein Eg5 | A, B | protein | 368 | Homo sapiens | P52732 (AlphaFold model) |
>1II6_1 KINESIN-RELATED MOTOR PROTEIN Eg5 (chains A, B) MASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADK SSRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERS PNEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSE RLQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFS VTIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVIT ALVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNIL NKPEVNQK
Water and common crystallization additives (NO3) are not listed.
Crystal structure of the mitotic spindle kinesin Eg5 reveals a novel conformation of the neck-linker. Turner, J., Anderson, R., Guo, J. et al. J Biol Chem (2001) 276:25496-25502. DOI 10.1074/jbc.M100395200 · PubMed
Other PDB entries of the same protein (UniProt P52732 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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