NRas 1-169 Q61R in Complex with Shoc2 80-582. Determined by X-ray diffraction at 2.73 Å resolution. Released 2 Apr 2025.
Explore 9BTM in 3D Show helices and sheets RCSB PDB PDBe
9BTM contains 28 α-helices and 28 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 | 2-10 | 9 | 2 |
| α-helix | 16-25 | 10 | |
| β-strand | 38-46 | 9 | 2 |
| β-strand | 49-57 | 9 | 2 |
| α-helix | 68-74 | 7 | |
| β-strand | 77-83 | 7 | 2 |
| α-helix | 87-91 | 5 | |
| α-helix | 93-103 | 11 | |
| β-strand | 111-116 | 6 | 2 |
| α-helix | 127-137 | 11 | |
| β-strand | 141-143 | 3 | 2 |
| β-strand | 145 | 1 | 3 |
| β-strand | 150 | 1 | 3 |
| α-helix | 152-167 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 87-100 | 14 | |
| β-strand | 104-106 | 3 | 1 |
| α-helix | 117-121 | 5 | |
| β-strand | 127-129 | 3 | 1 |
| α-helix | 140-144 | 5 | |
| β-strand | 150-152 | 3 | 1 |
| α-helix | 163-167 | 5 | |
| β-strand | 173-175 | 3 | 1 |
| α-helix | 188-190 | 3 | |
| β-strand | 196-198 | 3 | 1 |
| α-helix | 209-213 | 5 | |
| β-strand | 219-221 | 3 | 1 |
| α-helix | 232-236 | 5 | |
| β-strand | 242-244 | 3 | 1 |
| α-helix | 255-259 | 5 | |
| β-strand | 265-267 | 3 | 1 |
| α-helix | 278-282 | 5 | |
| β-strand | 288-290 | 3 | 1 |
| α-helix | 301-305 | 5 | |
| β-strand | 311-313 | 3 | 1 |
| β-strand | 335-337 | 3 | 1 |
| α-helix | 346-347 | 2 | |
| α-helix | 351-353 | 3 | |
| β-strand | 359-361 | 3 | 1 |
| α-helix | 370-371 | 2 | |
| β-strand | 383-385 | 3 | 1 |
| α-helix | 396-400 | 5 | |
| β-strand | 406-408 | 3 | 1 |
| α-helix | 419-423 | 5 | |
| β-strand | 429-431 | 3 | 1 |
| α-helix | 442-446 | 5 | |
| β-strand | 452-454 | 3 | 1 |
| α-helix | 465-469 | 5 | |
| β-strand | 475-477 | 3 | 1 |
| α-helix | 488-492 | 5 | |
| β-strand | 498-500 | 3 | 1 |
| α-helix | 511-515 | 5 | |
| β-strand | 521-523 | 3 | 1 |
| α-helix | 535-539 | 5 | |
| β-strand | 545-547 | 3 | 1 |
| α-helix | 558-563 | 6 | |
| α-helix | 565-574 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Leucine-rich repeat protein SHOC-2 | B | protein | 503 | Homo sapiens | Q9UQ13 (AlphaFold model) |
| GTPase NRas | A | protein | 169 | Homo sapiens | P01111 (AlphaFold model) |
>9BTM_1 Leucine-rich repeat protein SHOC-2 (chains B) GTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLP AEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYL RFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEIGN CTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNI STLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAK VLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKK LPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTHL GLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQ IVAGGPSFIIQFLKMQGPYRAMV
>9BTM_2 GTPase NRas (chains A) MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG REEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDL PTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMK
Targeting the SHOC2-RAS interaction in RAS-mutant cancers. Hauseman, Z.J., Stauffer, F., Beyer, K.S. et al. Nature (2025) 642:232-241. DOI 10.1038/s41586-025-08931-1 · PubMed
Other PDB entries of the same protein (UniProt Q9UQ13 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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