7SD0: SHOC2:PP1C:MRAS complex

Cryo-EM structure of the SHOC2:PP1C:MRAS complex. Determined by electron microscopy at 2.95 Å resolution. Released 20 Apr 2022.

Method: Electron microscopy
Resolution: 2.95 Å
Organism: Homo sapiens
Chains: 3
Atoms: 7,729
Mol. weight: 127.02 kDa
Ligands: MN, MG, GCP
Released: 20 Apr 2022

Explore 7SD0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7SD0 contains 43 α-helices and 52 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: 21 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	65-66	2	1
α-helix	87-100	14
β-strand	104-106	3	2
α-helix	117-121	5
β-strand	127-129	3	2
β-strand	137	1	3
α-helix	142-144	3
β-strand	150-152	3	2
β-strand	160	1	3
α-helix	163-167	5
β-strand	173-175	3	2
α-helix	188-190	3
β-strand	196-198	3	2
β-strand	219-222	4	2
α-helix	232-236	5
β-strand	242-245	4	2
α-helix	255-259	5
β-strand	265-267	3	2
α-helix	278-282	5
β-strand	288-290	3	2
α-helix	301-305	5
β-strand	311-313	3	2
α-helix	325-328	4
β-strand	335-337	3	2
α-helix	346-347	2
α-helix	351-354	4
β-strand	359-361	3	2
α-helix	369-371	3
α-helix	396-400	5
β-strand	406	1	4
α-helix	419-423	5
β-strand	429-431	3	4
α-helix	442-446	5
β-strand	452-454	3	4
α-helix	465-468	4
β-strand	475-477	3	4
β-strand	498-500	3	4
α-helix	511-515	5
β-strand	521-523	3	4
α-helix	536-539	4
β-strand	545-547	3	4
α-helix	558-563	6
α-helix	565-573	9

Chain B: 8 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	5
α-helix	26-35	10
β-strand	48-49	2	5
β-strand	53-55	3	5
β-strand	60-67	8	5
α-helix	75-77	3
α-helix	78-83	6
β-strand	87-93	7	5
α-helix	97-114	18
β-strand	121-126	6	5
α-helix	131-133	3
α-helix	138-147	10
β-strand	152-154	3	5
β-strand	156	1	6
α-helix	161	1
β-strand	162	1	6
α-helix	164-177	14

Chain C: 14 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-55	4	7
β-strand	59-61	3	1
β-strand	64	1	8
β-strand	68	1	9
α-helix	69-79	11
β-strand	87-89	3	1
β-strand	99	1	9
α-helix	101-113	13
β-strand	118-120	3	1
α-helix	124-126	3
α-helix	130-133	4
α-helix	136-143	8
α-helix	147-156	10
β-strand	162-165	4	7
β-strand	169-171	3	7
α-helix	183-187	5
α-helix	200-206	7
β-strand	209	1	10
β-strand	218	1	11
β-strand	225	1	11
β-strand	227	1	10
α-helix	229-239	11
β-strand	243-246	4	7
β-strand	255-258	4	7
β-strand	263-266	4	7
β-strand	267	1	8
α-helix	272-274	3
β-strand	280	1	12
β-strand	283-285	3	1
β-strand	290-293	4	1
α-helix	295	1
β-strand	296	1	12
α-helix	297	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Leucine-rich repeat protein SHOC-2	A	protein	585	Homo sapiens	Q9UQ13 (AlphaFold model)
Ras-related protein M-Ras	B	protein	210	Homo sapiens	O14807 (AlphaFold model)
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit	C	protein	325	Homo sapiens	P36873 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>7SD0_1 Leucine-rich repeat protein SHOC-2 (chains A)
GSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKDSSAA
QPGVAFSVDNTIKRPNPAPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIK
ELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNK
LREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNL
ITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIP
RSLAKCSALEELNLENNNISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSL
NMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPED
VSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTN
NQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALC
SKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMVGNS

Sequence of entity 2 (B), FASTA

>7SD0_2 Ras-related protein M-Ras (chains B)
GSMATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDN
QWAILDVLDTAGQEEFSAMREQYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRES
FPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQ
IPEKSQKKKKKTKWRGDRATGTHKLQCVIL

Sequence of entity 3 (C), FASTA

>7SD0_3 Serine/threonine-protein phosphatase PP1-gamma catalytic subunit (chains C)
GSMADLDKLNIDSIIQRLLEVRGSKPGKNVQLQENEIRGLCLKSREIFLSQPILLELEAP
LKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENF
FLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSP
DLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVLGWGENDRGVSFTFGAEVVAKFLHK
HDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP
AEKKKPNATRPVTPPRGMITKQAKK

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	2
MG	Magnesium ion	Mg	1
GCP	Phosphomethylphosphonic acid guanylate ester	C11 H18 N5 O13 P3	1

Primary citation

Structural basis for SHOC2 modulation of RAS signalling. Liau, N.P.D., Johnson, M.C., Izadi, S. et al. Nature (2022) 609:400-407. DOI 10.1038/s41586-022-04838-3 · 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
9O65 3.0 Å, Cryo-EM structure of SHOC2-KRAS-PP1CA (SKP) complex
7SD1 3.19 Å, Crystal structure of SHOC2

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