9BTM: NRas 1-169 Q61R

NRas 1-169 Q61R in Complex with Shoc2 80-582. Determined by X-ray diffraction at 2.73 Å resolution. Released 2 Apr 2025.

Method
X-ray diffraction
Resolution
2.73 Å
Organism
Homo sapiens
Chains
2
Atoms
5,252
Mol. weight
76.37 kDa
Ligands
MG, GTP
Released
2 Apr 2025

Explore 9BTM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 6 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand2-1092
α-helix16-2510
β-strand38-4692
β-strand49-5792
α-helix68-747
β-strand77-8372
α-helix87-915
α-helix93-10311
β-strand111-11662
α-helix127-13711
β-strand141-14332
β-strand14513
β-strand15013
α-helix152-16716
Chain B: 22 helices, 20 β-strands
ElementResiduesLengthSheet
α-helix87-10014
β-strand104-10631
α-helix117-1215
β-strand127-12931
α-helix140-1445
β-strand150-15231
α-helix163-1675
β-strand173-17531
α-helix188-1903
β-strand196-19831
α-helix209-2135
β-strand219-22131
α-helix232-2365
β-strand242-24431
α-helix255-2595
β-strand265-26731
α-helix278-2825
β-strand288-29031
α-helix301-3055
β-strand311-31331
β-strand335-33731
α-helix346-3472
α-helix351-3533
β-strand359-36131
α-helix370-3712
β-strand383-38531
α-helix396-4005
β-strand406-40831
α-helix419-4235
β-strand429-43131
α-helix442-4465
β-strand452-45431
α-helix465-4695
β-strand475-47731
α-helix488-4925
β-strand498-50031
α-helix511-5155
β-strand521-52331
α-helix535-5395
β-strand545-54731
α-helix558-5636
α-helix565-57410

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Leucine-rich repeat protein SHOC-2Bprotein503Homo sapiensQ9UQ13 (AlphaFold model)
GTPase NRasAprotein169Homo sapiensP01111 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>9BTM_1 Leucine-rich repeat protein SHOC-2 (chains B)
GTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQSLP
AEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTLYL
RFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEIGN
CTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENNNI
STLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSRAK
VLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLLKK
LPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLTHL
GLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLPPQ
IVAGGPSFIIQFLKMQGPYRAMV
Sequence of entity 2 (A), FASTA
>9BTM_2 GTPase NRas (chains A)
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
REEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKCDL
PTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMK

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
GTPGuanosine-5'-triphosphateC10 H16 N5 O14 P31

Primary citation

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:

Browse structure collections

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