Crystal structure of the motor protein KSP in complex with ADP and monastrol. Determined by X-ray diffraction at 1.9 Å resolution. Released 13 Jan 2004.
Explore 1Q0B in 3D Show helices and sheets RCSB PDB PDBe
1Q0B contains 46 α-helices and 40 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 | 17-18 | 2 | 1 |
| α-helix | 19 | 1 | |
| β-strand | 20-25 | 6 | 2 |
| α-helix | 26-28 | 3 | |
| α-helix | 30-34 | 5 | |
| α-helix | 37-38 | 2 | |
| β-strand | 39 | 1 | 3 |
| β-strand | 41-44 | 4 | 4 |
| α-helix | 45-47 | 3 | |
| β-strand | 49-56 | 8 | 4 |
| β-strand | 61-67 | 7 | 4 |
| β-strand | 70-72 | 3 | 2 |
| α-helix | 78-81 | 4 | |
| α-helix | 82-86 | 5 | |
| α-helix | 87-94 | 8 | |
| β-strand | 98-105 | 8 | 2 |
| α-helix | 111-115 | 5 | |
| β-strand | 117 | 1 | 5 |
| α-helix | 119-120 | 2 | |
| α-helix | 121-123 | 3 | |
| β-strand | 133 | 1 | 5 |
| α-helix | 135-149 | 15 | |
| β-strand | 152-164 | 13 | 2 |
| β-strand | 167-170 | 4 | 2 |
| α-helix | 180-181 | 2 | |
| β-strand | 182 | 1 | 2 |
| β-strand | 183-186 | 4 | 6 |
| β-strand | 194-197 | 4 | 6 |
| β-strand | 202-203 | 2 | 2 |
| α-helix | 207-209 | 3 | |
| α-helix | 210-227 | 18 | |
| α-helix | 231-234 | 4 | |
| β-strand | 236-248 | 13 | 2 |
| β-strand | 254-265 | 12 | 2 |
| α-helix | 266-268 | 3 | |
| α-helix | 290-303 | 14 | |
| α-helix | 311-313 | 3 | |
| α-helix | 315-319 | 5 | |
| α-helix | 321-323 | 3 | |
| β-strand | 329-336 | 8 | 2 |
| β-strand | 339 | 1 | 3 |
| α-helix | 340-342 | 3 | |
| α-helix | 343-356 | 14 | |
| β-strand | 360-361 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17-18 | 2 | 7 |
| α-helix | 19 | 1 | |
| β-strand | 20-25 | 6 | 8 |
| α-helix | 26-29 | 4 | |
| α-helix | 30-33 | 4 | |
| α-helix | 37-39 | 3 | |
| β-strand | 41-44 | 4 | 9 |
| β-strand | 49-56 | 8 | 9 |
| β-strand | 61-67 | 7 | 9 |
| β-strand | 70-72 | 3 | 8 |
| α-helix | 78-81 | 4 | |
| α-helix | 82-86 | 5 | |
| α-helix | 87-94 | 8 | |
| β-strand | 98-105 | 8 | 8 |
| α-helix | 111-115 | 5 | |
| β-strand | 117 | 1 | 10 |
| α-helix | 119-120 | 2 | |
| α-helix | 121-123 | 3 | |
| α-helix | 127-129 | 3 | |
| β-strand | 133 | 1 | 10 |
| α-helix | 135-146 | 12 | |
| β-strand | 152-164 | 13 | 8 |
| β-strand | 167-170 | 4 | 8 |
| α-helix | 180-181 | 2 | |
| β-strand | 182 | 1 | 8 |
| β-strand | 183-186 | 4 | 11 |
| β-strand | 194-197 | 4 | 11 |
| β-strand | 202-204 | 3 | 8 |
| α-helix | 207-209 | 3 | |
| α-helix | 210-227 | 18 | |
| α-helix | 231-234 | 4 | |
| β-strand | 236-248 | 13 | 8 |
| β-strand | 254-265 | 12 | 8 |
| α-helix | 266-268 | 3 | |
| α-helix | 290-303 | 14 | |
| α-helix | 311-313 | 3 | |
| α-helix | 315-319 | 5 | |
| α-helix | 321-323 | 3 | |
| β-strand | 329-336 | 8 | 8 |
| α-helix | 340-342 | 3 | |
| α-helix | 343-356 | 14 | |
| β-strand | 360-361 | 2 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinesin-like protein KIF11 | A, B | protein | 367 | Homo sapiens | P52732 (AlphaFold model) |
>1Q0B_1 Kinesin-like protein KIF11 (chains A, B) ASQPNSSAKKKEEKGKNIQVVVRCRPFNLAERKASAHSIVECDPVRKEVSVRTGGLADKS SRKTYTFDMVFGASTKQIDVYRSVVCPILDEVIMGYNCTIFAYGQTGTGKTFTMEGERSP NEEYTWEEDPLAGIIPRTLHQIFEKLTDNGTEFSVKVSLLEIYNEELFDLLNPSSDVSER LQMFDDPRNKRGVIIKGLEEITVHNKDEVYQILEKGAAKRTTAATLMNAYSSRSHSVFSV TIHMKETTIDGEELVKIGKLNLVDLAGSENIGRSGAVDKRAREAGNINQSLLTLGRVITA LVERTPHVPYRESKLTRILQDSLGGRTRTSIIATISPASLNLEETLSTLEYAHRAKNILN KPEVNQK
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
| ADP | Adenosine-5'-diphosphate | C10 H15 N5 O10 P2 | 2 |
| NAT | Ethyl 4-(3-hydroxyphenyl)-6-methyl-2-thioxo-1,2,3,4-tetrahydropyrimidine-5-carb… | C14 H16 N2 O3 S | 2 |
Inhibition of a mitotic motor protein: where, how, and conformational consequences. Yan, Y., Sardana, V., Xu, B. et al. J Mol Biol (2004) 335:547-554. DOI 10.1016/j.jmb.2003.10.074 · 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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