7TVF: PDB entry 7TVF

Crystal structure of the SHOC2-MRAS-PP1CA (SMP) complex to a resolution of 2.17 Angstrom. Determined by X-ray diffraction at 2.17 Å resolution. Released 4 May 2022.

Method: X-ray diffraction
Resolution: 2.17 Å
Organism: Homo sapiens
Chains: 6
Atoms: 16,911
Mol. weight: 249.1 kDa
Ligands: MN, PO4, GNP, MG
Released: 4 May 2022

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

Secondary structure: helices and β-sheets

7TVF contains 88 α-helices and 92 β-strands across 6 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	65-68	4	6
β-strand	71-73	3	6
α-helix	88-100	13
β-strand	104-106	3	13
α-helix	117-121	5
β-strand	127-129	3	13
α-helix	140-144	5
β-strand	150-152	3	13
α-helix	163-167	5
β-strand	173-175	3	13
α-helix	188-190	3
β-strand	196-198	3	13
α-helix	209-213	5
β-strand	219-221	3	13
α-helix	232-236	5
β-strand	242-244	3	13
α-helix	255-259	5
β-strand	265-267	3	13
α-helix	278-282	5
β-strand	288-290	3	13
α-helix	301-305	5
β-strand	312-313	2	13
α-helix	326-329	4
β-strand	335-337	3	13
α-helix	346-348	3
β-strand	359-361	3	13
β-strand	383-385	3	13
α-helix	398-400	3
β-strand	406-408	3	13
α-helix	419-423	5
β-strand	429-431	3	13
α-helix	442-446	5
β-strand	452-454	3	13
α-helix	465-469	5
β-strand	475-477	3	13
α-helix	488-492	5
β-strand	498-500	3	13
α-helix	511-515	5
β-strand	521-523	3	13
α-helix	535-539	5
β-strand	545-547	3	13
α-helix	558-563	6
α-helix	565-574	10

Chain B: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	7-8	2
β-strand	13-20	8	11
α-helix	26-35	10
β-strand	47-56	10	11
β-strand	59-68	10	11
α-helix	72-74	3
α-helix	78-83	6
β-strand	87-93	7	11
α-helix	97-101	5
α-helix	103-114	12
β-strand	121-126	6	11
α-helix	131-133	3
α-helix	138-148	11
β-strand	152-154	3	11
β-strand	156	1	12
α-helix	161	1
β-strand	162	1	12
α-helix	164-176	13

Chain C: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	18-20	3
α-helix	32-48	17
β-strand	52-55	4	5
β-strand	59-62	4	6
β-strand	64	1	7
α-helix	69-79	11
β-strand	87-89	3	6
α-helix	100-113	14
β-strand	118-120	3	6
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	5
β-strand	169-172	4	5
α-helix	184-187	4
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	8
β-strand	216-218	3	8
β-strand	225-227	3	8
α-helix	229-239	11
β-strand	243-246	4	5
β-strand	255-258	4	5
β-strand	263-266	4	5
β-strand	267	1	7
α-helix	272-274	3
β-strand	280-285	6	6
β-strand	290-296	7	6

Chain D: 23 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	65-68	4	2
β-strand	71-73	3	2
α-helix	83-100	18
β-strand	104-106	3	14
α-helix	117-121	5
β-strand	127-129	3	14
α-helix	140-144	5
β-strand	150-152	3	14
α-helix	163-167	5
β-strand	173-175	3	14
α-helix	188-190	3
β-strand	196-198	3	14
α-helix	209-213	5
β-strand	219-221	3	14
α-helix	232-236	5
β-strand	242-244	3	14
α-helix	255-259	5
β-strand	265-267	3	14
α-helix	278-282	5
β-strand	288-290	3	14
α-helix	301-305	5
β-strand	311-313	3	15
α-helix	327-329	3
β-strand	335-337	3	15
α-helix	346-348	3
α-helix	351-354	4
β-strand	359-361	3	15
α-helix	370-371	2
β-strand	383-385	3	15
α-helix	398-400	3
β-strand	406-408	3	15
α-helix	419-423	5
β-strand	429-431	3	15
α-helix	442-446	5
β-strand	452-454	3	15
α-helix	465-469	5
β-strand	475-477	3	15
α-helix	488-492	5
β-strand	498-500	3	15
α-helix	511-515	5
β-strand	521-523	3	15
α-helix	535-539	5
β-strand	545-547	3	15
α-helix	558-563	6
α-helix	565-574	10

Chain E: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-20	8	9
α-helix	26-35	10
β-strand	47-56	10	9
β-strand	59-68	10	9
α-helix	72-74	3
α-helix	78-83	6
β-strand	87-93	7	9
α-helix	97-101	5
α-helix	103-114	12
β-strand	121-126	6	9
α-helix	131-133	3
α-helix	138-148	11
β-strand	152-154	3	9
β-strand	156	1	10
α-helix	161	1
β-strand	162	1	10
α-helix	164-176	13

Chain F: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-55	4	1
β-strand	59-62	4	2
β-strand	64	1	3
α-helix	69-79	11
β-strand	87-89	3	2
α-helix	100-113	14
β-strand	118-120	3	2
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	1
β-strand	169-172	4	1
α-helix	184-187	4
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	4
β-strand	216-218	3	4
β-strand	225-227	3	4
α-helix	229-238	10
β-strand	243-246	4	1
β-strand	255-258	4	1
β-strand	263-266	4	1
β-strand	267	1	3
α-helix	272-274	3
β-strand	280-285	6	2
β-strand	290-296	7	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	C, F	protein	329	Homo sapiens	P62136 (AlphaFold model)
Ras-related protein M-Ras	B, E	protein	179	Homo sapiens	O14807 (AlphaFold model)
Leucine-rich repeat protein SHOC-2	A, D	protein	582	Homo sapiens	Q9UQ13 (AlphaFold model)

Sequence of entity 1 (C, F), FASTA

>7TVF_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains C, F)
SDSEKLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKI
CGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL
RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ
SMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDL
DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADK
NKGKYGQFSGLNPGGRPITPPRNSAKAKK

Sequence of entity 2 (B, E), FASTA

>7TVF_2 Ras-related protein M-Ras (chains B, E)
GMATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQ
WAILDVLDTAGLEEFSAMREQYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESF
PMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQ

Sequence of entity 3 (A, D), FASTA

>7TVF_3 Leucine-rich repeat protein SHOC-2 (chains A, D)
GSSSLGKEKDSKEKDPKVPSAKEREKEAKASGGFGKESKEKEPKTKGKDAKDGKKDSSAA
QPGVAFSVDNTIKRPNPAPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIK
ELTQLTELYLYSNKLQSLPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRMLDLRHNK
LREIPSVVYRLDSLTTLYLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNL
ITLDVAHNQLEHLPKEIGNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIP
RSLAKCSALEELNLENNNISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSL
NMEHNRINKIPFGIFSRAKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPED
VSGLVSLEVLILSNNLLKKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTN
NQLTTLPRGIGHLTNLTHLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALC
SKLSIMSIENCPLSHLPPQIVAGGPSFIIQFLKMQGPYRAMV

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	4
PO4	Phosphate ion	O4 P	1
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	2
MG	Magnesium ion	Mg	2

Water and common crystallization additives (GOL, SO4, NA, CL) are not listed.

Primary citation

Structure of the SHOC2-MRAS-PP1C complex provides insights into RAF activation and Noonan syndrome. Bonsor, D.A., Alexander, P., Snead, K. et al. Nat Struct Mol Biol (2022) 29:966-977. DOI 10.1038/s41594-022-00841-4 · PubMed

Other PDB entries of the same protein (UniProt P62136 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ZEG 1.09 Å, Structure of PP1-IRSp53 chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)] bound to…
6ZEH 1.3 Å, Structure of PP1-spectrin alpha II chimera [PP1(7-304) + linker (G/S)x9 + spectrin alpha…
6ZEI 1.39 Å, Structure of PP1-IRSp53 S455E chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)]…
6DNO 1.45 Å, Crystal structure of Protein Phosphatase 1 (PP1) bound to the muscle glycogen-targeting…
4MOV 1.45 Å, 1.45 A Resolution Crystal Structure of Protein Phosphatase 1
6OBR 1.5 Å, PP1 Y134A in complex with Microcystin LR
3E7A 1.63 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin Nodularin-R
3E7B 1.7 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin inhibitor Tautomycin
8SW6 1.76 Å, Protein Phosphatase 1 in complex with PP1-specific Phosphatase targeting peptide…
6ZEJ 1.78 Å, Structure of PP1-Phactr1 chimera [PP1(7-304) + linker (SGSGS) + Phactr1(526-580)]
7T0Y 1.8 Å, The Ribosomal RNA Processing 1B Protein Phosphatase-1 Holoenzyme
6OBS 1.8 Å, PP1 Y134K

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