Crystal Structure of KSR2:MEK1 in complex with AMP-PNP, and allosteric MEK inhibitor Trametinib. Determined by X-ray diffraction at 2.82 Å resolution. Released 30 Sept 2020.
Explore 7JUR in 3D Show helices and sheets RCSB PDB PDBe
7JUR contains 35 α-helices and 24 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 | 654 | 1 | 1 |
| α-helix | 656-658 | 3 | |
| β-strand | 667-673 | 7 | 1 |
| β-strand | 679-684 | 6 | 1 |
| β-strand | 688-695 | 8 | 1 |
| α-helix | 701-714 | 14 | |
| β-strand | 719 | 1 | 2 |
| β-strand | 722 | 1 | 2 |
| β-strand | 725-727 | 3 | 1 |
| β-strand | 730-731 | 2 | 1 |
| β-strand | 734-740 | 7 | 1 |
| α-helix | 741-743 | 3 | |
| β-strand | 745-746 | 2 | 2 |
| α-helix | 747-751 | 5 | |
| α-helix | 760-779 | 20 | |
| α-helix | 789-791 | 3 | |
| β-strand | 792-795 | 4 | 2 |
| β-strand | 798-801 | 4 | 2 |
| α-helix | 806-809 | 4 | |
| β-strand | 821-825 | 5 | 3 |
| α-helix | 829-831 | 3 | |
| α-helix | 834-837 | 4 | |
| α-helix | 846-848 | 3 | |
| α-helix | 853-869 | 17 | |
| α-helix | 879-887 | 9 | |
| α-helix | 895-897 | 3 | |
| α-helix | 901-910 | 10 | |
| α-helix | 915-917 | 3 | |
| α-helix | 919-920 | 2 | |
| α-helix | 921-929 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-53 | 10 | |
| α-helix | 65-67 | 3 | |
| β-strand | 68-73 | 6 | 4 |
| β-strand | 82-87 | 6 | 4 |
| β-strand | 93-97 | 5 | 4 |
| β-strand | 99-100 | 2 | 4 |
| α-helix | 106-115 | 10 | |
| α-helix | 117-120 | 4 | |
| β-strand | 126 | 1 | 5 |
| β-strand | 129-134 | 6 | 4 |
| β-strand | 138-144 | 7 | 4 |
| β-strand | 149-150 | 2 | 5 |
| α-helix | 151-157 | 7 | |
| α-helix | 163-184 | 22 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 5 |
| β-strand | 204-206 | 3 | 5 |
| α-helix | 213-218 | 6 | |
| β-strand | 221-225 | 5 | 3 |
| α-helix | 232-235 | 4 | |
| α-helix | 243-258 | 16 | |
| α-helix | 265-267 | 3 | |
| α-helix | 268-274 | 7 | |
| α-helix | 310-319 | 10 | |
| α-helix | 321-323 | 3 | |
| α-helix | 332-341 | 10 | |
| α-helix | 359-365 | 7 | |
| α-helix | 371-375 | 5 | |
| α-helix | 376-380 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinase suppressor of Ras 2 | B | protein | 342 | Homo sapiens | Q6VAB6 (AlphaFold model) |
| Dual specificity mitogen-activated protein kinase kinase 1 | C | protein | 384 | Oryctolagus cuniculus | P29678 (AlphaFold model) |
>7JUR_1 Kinase suppressor of Ras 2 (chains B) MSYYHHHHHHDYDIPTTENLYFQGAEMNLSLLSARSFPRKASQTSIFLQEWDIPFEQLEI GELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGA CMSPPHLAIITSLCKGRTLYSVVRDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLK SKNVFYDNGKVVITDFGLFSISGVLQAGRREDKLRIQNGWLCHLAPEIIRQLSPDTEEDK LPFSKHSDVFALGTIWYELHAREWPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEISDILL FCWAFEQEERPTFTKLMDMLEKLPKRNRRLSHPGHFWKSAEL
>7JUR_2 Dual specificity mitogen-activated protein kinase kinase 1 (chains C) MSYYHHHHHHDYDIPTTENLYFQGAKKLEELELDEQQRKRLEAFLTQKQKVGELKDDDFE KISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGF YGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHKIMHR DVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGTHYSVQSDIWSM GLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSRPPMA IFELLDYIVNEPPPKLPSAVFSLEFQDFVNKCLIKNPAERADLKQLMVHAFIKRSDAEEV DFAGWLCSTIGLNQPSTPTHAAGV
| ID | Name | Formula | Copies |
|---|---|---|---|
| QOM | Trametinib | C26 H23 F I N5 O4 | 1 |
| MG | Magnesium ion | Mg | 2 |
| ANP | Phosphoaminophosphonic acid-adenylate ester | C10 H17 N6 O12 P3 | 2 |
Structural basis for the action of the drug trametinib at KSR-bound MEK. Khan, Z.M., Real, A.M., Marsiglia, W.M. et al. Nature (2020) 588:509-514. DOI 10.1038/s41586-020-2760-4 · PubMed
Other PDB entries of the same protein (UniProt Q6VAB6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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