KSR2-MEK1 heterodimer. Determined by X-ray diffraction at 3.46 Å resolution. Released 19 Jan 2011.
Explore 2Y4I in 3D Show helices and sheets RCSB PDB PDBe
2Y4I contains 34 α-helices and 29 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 | 666-667 | 2 | 1 |
| β-strand | 671 | 1 | 2 |
| β-strand | 679-683 | 5 | 2 |
| β-strand | 684-685 | 2 | 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 | 727-730 | 4 | 2 |
| β-strand | 735-738 | 4 | 2 |
| β-strand | 740 | 1 | 2 |
| α-helix | 741-742 | 2 | |
| β-strand | 745-746 | 2 | 3 |
| α-helix | 747-750 | 4 | |
| α-helix | 761-779 | 19 | |
| β-strand | 792-794 | 3 | 3 |
| β-strand | 800-801 | 2 | 3 |
| β-strand | 823 | 1 | 4 |
| α-helix | 827-830 | 4 | |
| α-helix | 834-837 | 4 | |
| β-strand | 840 | 1 | 5 |
| α-helix | 853-869 | 17 | |
| α-helix | 879-887 | 9 | |
| α-helix | 891-893 | 3 | |
| α-helix | 903-911 | 9 | |
| α-helix | 919-920 | 2 | |
| α-helix | 921-928 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-55 | 12 | |
| β-strand | 68-69 | 2 | 6 |
| β-strand | 73-75 | 3 | 7 |
| β-strand | 82-83 | 2 | 7 |
| β-strand | 86-87 | 2 | 6 |
| β-strand | 92 | 1 | 6 |
| β-strand | 95-100 | 6 | 7 |
| α-helix | 105-115 | 11 | |
| α-helix | 116-120 | 5 | |
| β-strand | 123 | 1 | 8 |
| β-strand | 126 | 1 | 8 |
| β-strand | 129-133 | 5 | 7 |
| β-strand | 138-143 | 6 | 7 |
| β-strand | 150 | 1 | 8 |
| α-helix | 151-156 | 6 | |
| α-helix | 163-184 | 22 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 8 |
| β-strand | 204-206 | 3 | 8 |
| α-helix | 213-218 | 6 | |
| β-strand | 223 | 1 | 4 |
| α-helix | 232-236 | 5 | |
| α-helix | 242-258 | 17 | |
| α-helix | 265-266 | 2 | |
| α-helix | 271-273 | 3 | |
| β-strand | 309 | 1 | 5 |
| α-helix | 310-319 | 10 | |
| α-helix | 321-323 | 3 | |
| α-helix | 325-326 | 2 | |
| α-helix | 332-341 | 10 | |
| α-helix | 350-351 | 2 | |
| α-helix | 352-356 | 5 | |
| α-helix | 359-366 | 8 | |
| 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) |
>2Y4I_1 KINASE SUPPRESSOR OF RAS 2 (chains B) GPEMNLSLLSARSFPRKASQTSIFLQEWDIPFEQLEIGELIGKGRFGQVYHGRWHGEVAI RLIDIERDNEDQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITSLCKGRTLYSVV RDAKIVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNGKVVITDFGLFSISG VLQAGRREDKLRIQNGWLCHLAPEIIRQLSPDTEEDKLPFSKHSDVFALGTIWYELHARE WPFKTQPAEAIIWQMGTGMKPNLSQIGMGKEISDILLFCWAFEQEERPTFTKLMDMLEKL PKRNRRLSHPGHFWKSAEL
>2Y4I_2 DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 1 (chains C) GPMPKKKPTPIQLNPAPDGSAVNGTSSAETNLEALQKKLLELELDEQQRKRLEAFLTQKQ KVGELKDDDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVL HECNSPYIVGFYGAFYSDGEISICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLT YLREKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSMANSFVGTRSYMSPERLQGT HYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGRPLS SYGMDSRPPMAIFELLDYIVNEPPPKLPSAVFSLEFQDFVNKCLIKNPAERADLKQLMVH AFIKRSDAEEVDFAGWLCSTIGLNQPSTPTHAAGV
Water and common crystallization additives (CL) are not listed.
A Raf-Induced Allosteric Transition of Ksr Stimulates Ksr and Raf Phosphorylation of Mek. Brennan, D.F., Dar, A.C., Hertz, N.T. et al. Nature (2011) 472:366. DOI 10.1038/NATURE09860 · 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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