9BTN: Human SHOC2

Structure of human SHOC2 in complex with a cyclic peptide. Determined by X-ray diffraction at 2.04 Å resolution. Released 2 Apr 2025.

Method: X-ray diffraction
Resolution: 2.04 Å
Organisms: Homo sapiens, synthetic construct
Chains: 2
Atoms: 4,247
Mol. weight: 58.65 kDa
Released: 2 Apr 2025

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

Secondary structure: helices and β-sheets

9BTN contains 23 α-helices and 22 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: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	87-99	13
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	186-190	5
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
α-helix	326-329	4
β-strand	335-337	3	1
α-helix	346-347	2
α-helix	351-354	4
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	558-562	5
α-helix	565-574	10

Chain L: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	2	1	2
β-strand	8	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Leucine-rich repeat protein SHOC-2	A	protein	505	Homo sapiens	Q9UQ13 (AlphaFold model)
cyclic peptide	L	protein	15	synthetic construct

Sequence of entity 1 (A), FASTA

>9BTN_1 Leucine-rich repeat protein SHOC-2 (chains A)
GPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQS
LPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNKLREIPSVVYRLDSLTTL
YLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEI
GNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENN
NISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSR
AKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLL
KKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLT
HLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLP
PQIVAGGPSFIIQFLKMQGPYRAMV

Sequence of entity 2 (L), FASTA

>9BTN_2 cyclic peptide (chains L)
FKDWYGEIWFDGVCX

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:

7T7A 1.79 Å, Crystal Structure of Human SHOC2: A Leucine-Rich Repeat Protein
7TYG 1.9 Å, Structure of the human leucine rich repeat protein SHOC2, residues 80-582
7TXH 1.95 Å, Human MRas Q71R in complex with human Shoc2 LRR domain M173I and human PP1Ca
7TVF 2.17 Å, Crystal structure of the SHOC2-MRAS-PP1CA (SMP) complex to a resolution of 2.17 Angstrom
9BTP 2.37 Å, Structure of human SHOC2 in complex with a small molecule inhibitor (S)-5
7TVG 2.4 Å, Crystal Structure of SHOC2 to a resolution of 2.4 Angstrom
9OVJ 2.68 Å, Structure of human SHOC2 in complex with a small molecule inhibitor (R)-5
9BTM 2.73 Å, NRas 1-169 Q61R in Complex with Shoc2 80-582
7UPI 2.89 Å, Cryo-EM structure of SHOC2-PP1c-MRAS holophosphatase complex
7SD0 2.95 Å, Cryo-EM structure of the SHOC2:PP1C:MRAS complex
9O65 3.0 Å, Cryo-EM structure of SHOC2-KRAS-PP1CA (SKP) complex
7SD1 3.19 Å, Crystal structure of SHOC2

Browse structure collections

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