9O65: SHOC2-KRAS-PP1CA (SKP) complex

Cryo-EM structure of SHOC2-KRAS-PP1CA (SKP) complex. Determined by electron microscopy at 3.0 Å resolution. Released 21 Jan 2026.

Method: Electron microscopy
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 3
Atoms: 7,348
Mol. weight: 122.46 kDa
Ligands: MN, MG, GNP
Released: 21 Jan 2026

Explore 9O65 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9O65 contains 38 α-helices and 42 β-strands across 3 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: 20 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	65-66	2	1
α-helix	88-100	13
β-strand	105-106	2	2
α-helix	117-121	5
β-strand	127-129	3	2
α-helix	140-144	5
β-strand	150-152	3	2
α-helix	163-167	5
β-strand	173-175	3	2
α-helix	186-190	5
β-strand	196-198	3	2
α-helix	209-213	5
β-strand	219-221	3	2
α-helix	232-236	5
β-strand	242-244	3	2
α-helix	255-259	5
β-strand	265-267	3	2
α-helix	280-282	3
β-strand	288-290	3	2
α-helix	301-305	5
β-strand	311-313	3	3
α-helix	326-329	4
β-strand	335-337	3	3
α-helix	346-347	2
α-helix	351-354	4
β-strand	359-361	3	3
α-helix	370-371	2
β-strand	383-385	3	3
α-helix	396-400	5
β-strand	406-408	3	3
α-helix	419-423	5
β-strand	429-431	3	3
α-helix	442-446	5
β-strand	452-454	3	3
α-helix	465-469	5
β-strand	475-477	3	3
β-strand	485	1	4
α-helix	488-492	5
β-strand	498-500	3	3
β-strand	508	1	4
α-helix	511-515	5
β-strand	521-523	3	3

Chain B: 7 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	5
α-helix	16-25	10
β-strand	38-46	9	5
β-strand	49-57	9	5
α-helix	62-64	3
α-helix	68-74	7
β-strand	77-83	7	5
α-helix	87-91	5
α-helix	93-104	12
β-strand	111-116	6	5
α-helix	127-137	11
β-strand	141-143	3	5
α-helix	152-166	15

Chain C: 11 helices, 14 β-strands

Element	Residues	Length	Sheet
α-helix	9-18	10
α-helix	19-21	3
α-helix	32-47	16
β-strand	52-55	4	6
β-strand	59-62	4	1
α-helix	69-79	11
β-strand	87-89	3	1
α-helix	100-113	14
β-strand	118-120	3	1
α-helix	128-134	7
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	6
β-strand	169-171	3	6
α-helix	183-187	5
α-helix	200-206	7
β-strand	208-209	2	7
β-strand	216-217	2	7
β-strand	226-227	2	7
α-helix	229-239	11
β-strand	243-246	4	6
β-strand	255-258	4	6
β-strand	263-266	4	6
β-strand	280-285	6	1
β-strand	290-296	7	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Leucine-rich repeat protein SHOC-2	A	protein	582	Homo sapiens	Q9UQ13 (AlphaFold model)
Isoform 2B of GTPase KRas	B	protein	169	Homo sapiens	P01116 (AlphaFold model)
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	C	protein	330	Homo sapiens	P62136 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9O65_1 Leucine-rich repeat protein SHOC-2 (chains A)
MSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKDSSAA
QPGVAFSVDNTIKRPNPAPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIK
ELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRILDLRHNK
LREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNL
ITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIP
RSLAKCSALEELNLENNNISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSL
NMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPED
VSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTN
NQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALC
SKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV

Sequence of entity 2 (B), FASTA

>9O65_2 Isoform 2B of GTPase KRas (chains B)
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
REEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDL
PSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEK

Sequence of entity 3 (C), FASTA

>9O65_3 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains C)
GSDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQRILLELEAPLK
ICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFL
LRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDL
QSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHD
LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD
KNKGKYGQFSGLNPGGRPITPPRNSAKAKK

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	2
MG	Magnesium ion	Mg	1
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1

Primary citation

Structure of SHOC2-KRAS-PP1C complex reveals RAS isoform-specific determinants and insights into targeting complex assembly by RAS inhibitors. Bonsor, D.A., Finci, L.I., Potter, J.R. et al. Nat Commun (2026) 17:1614-1614. DOI 10.1038/s41467-026-68319-1 · 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
9BTN 2.04 Å, Structure of human SHOC2 in complex with a cyclic peptide
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
7SD1 3.19 Å, Crystal structure of SHOC2

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