KSR2:MEK1 Complex Bound to the Small Molecule APS-2-79. Determined by X-ray diffraction at 3.51 Å resolution. Released 31 Aug 2016.
Explore 5KKR in 3D Show helices and sheets RCSB PDB PDBe
5KKR contains 34 α-helices and 27 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 |
|---|---|---|---|
| α-helix | 656-658 | 3 | |
| β-strand | 667 | 1 | 1 |
| β-strand | 671 | 1 | 2 |
| β-strand | 679-681 | 3 | 2 |
| β-strand | 684 | 1 | 1 |
| β-strand | 688 | 1 | 1 |
| β-strand | 689-693 | 5 | 2 |
| α-helix | 696-697 | 2 | |
| α-helix | 704-708 | 5 | |
| α-helix | 711-714 | 4 | |
| β-strand | 722 | 1 | 3 |
| β-strand | 727-729 | 3 | 2 |
| β-strand | 736-740 | 5 | 2 |
| α-helix | 741-742 | 2 | |
| β-strand | 745-746 | 2 | 3 |
| α-helix | 747-751 | 5 | |
| α-helix | 760-780 | 21 | |
| α-helix | 789-791 | 3 | |
| β-strand | 792-794 | 3 | 3 |
| β-strand | 800-801 | 2 | 3 |
| β-strand | 823 | 1 | 4 |
| α-helix | 853-868 | 16 | |
| α-helix | 879-887 | 9 | |
| α-helix | 891-893 | 3 | |
| α-helix | 905-910 | 6 | |
| α-helix | 915-917 | 3 | |
| α-helix | 919-920 | 2 | |
| α-helix | 921-928 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-55 | 12 | |
| β-strand | 68-69 | 2 | 5 |
| β-strand | 73 | 1 | 6 |
| β-strand | 82-83 | 2 | 6 |
| β-strand | 86-87 | 2 | 5 |
| β-strand | 92-93 | 2 | 5 |
| β-strand | 95-100 | 6 | 6 |
| α-helix | 105-111 | 7 | |
| α-helix | 113-115 | 3 | |
| α-helix | 117-119 | 3 | |
| β-strand | 123 | 1 | 7 |
| β-strand | 126 | 1 | 7 |
| β-strand | 129-135 | 7 | 6 |
| β-strand | 138-143 | 6 | 6 |
| β-strand | 150 | 1 | 7 |
| α-helix | 151-158 | 8 | |
| α-helix | 163-182 | 20 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 7 |
| β-strand | 204-206 | 3 | 7 |
| α-helix | 213-218 | 6 | |
| β-strand | 223 | 1 | 4 |
| α-helix | 232-235 | 4 | |
| α-helix | 244-258 | 15 | |
| α-helix | 265-266 | 2 | |
| α-helix | 271-273 | 3 | |
| α-helix | 310-319 | 10 | |
| α-helix | 321-323 | 3 | |
| α-helix | 325-326 | 2 | |
| α-helix | 332-341 | 10 | |
| α-helix | 352-356 | 5 | |
| α-helix | 359-364 | 6 | |
| α-helix | 371-375 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinase suppressor of Ras 2 | B | protein | 319 | Homo sapiens | Q6VAB6 (AlphaFold model) |
| Dual specificity mitogen-activated protein kinase kinase 1 | C | protein | 395 | Oryctolagus cuniculus | P29678 (AlphaFold model) |
>5KKR_1 Kinase suppressor of Ras 2 (chains B) GAEMNLSLLSARSFPRKASQTSIFLQEWDIPFEQLEIGELIGKGRFGQVYHGRWHGEVAI RLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVV RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISG VLQAGRREDKLRIQNGWLCHLAPEIIRQLSPDTEEDKLPFSKHSDVFALGTIWYELHARE WPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL PKRNRRLSHPGHFWKSAEL
>5KKR_2 Dual specificity mitogen-activated protein kinase kinase 1 (chains C) GAMPKKKPTPIQLNPAPDGSAVNGTSSAETNLEALQKKLEELELDEQQRKRLEAFLTQKQ KVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVL HECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLT YLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGT HYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLS SYGMDSRPPMAIFELLDYIVNEPPPKLPSAVFSLEFQDFVNKCLIKNPAERADLKQLMVH AFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGV
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6U7 | 6,7-dimethoxy-~{N}-(2-methyl-4-phenoxy-phenyl)quinazolin-4-amine | C23 H21 N3 O3 | 1 |
Small molecule stabilization of the KSR inactive state antagonizes oncogenic Ras signalling. Dhawan, N.S., Scopton, A.P., Dar, A.C. Nature (2016) 537:112-116. DOI 10.1038/nature19327 · 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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