7TXH: Human MRas Q71R

Human MRas Q71R in complex with human Shoc2 LRR domain M173I and human PP1Ca. Determined by X-ray diffraction at 1.95 Å resolution. Released 22 Jun 2022.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 6
Atoms: 17,319
Mol. weight: 225.67 kDa
Ligands: GNP, MG, MN, PO4
Released: 22 Jun 2022

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

Secondary structure: helices and β-sheets

7TXH contains 89 α-helices and 89 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: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-20	8	1
α-helix	26-35	10
β-strand	47-56	10	1
β-strand	59-68	10	1
α-helix	72-74	3
α-helix	78-83	6
β-strand	87-93	7	1
α-helix	97-101	5
α-helix	103-114	12
β-strand	121-126	6	1
α-helix	131-133	3
α-helix	138-148	11
β-strand	152-155	4	1
β-strand	156	1	2
α-helix	161	1
β-strand	162	1	2
α-helix	164-176	13

Chain B: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	87-100	14
β-strand	104-106	3	3
α-helix	117-121	5
β-strand	127-129	3	3
α-helix	140-144	5
β-strand	150-152	3	3
α-helix	163-167	5
β-strand	173-175	3	3
α-helix	188-190	3
β-strand	196-198	3	3
α-helix	209-213	5
β-strand	219-221	3	3
α-helix	232-236	5
β-strand	242-244	3	3
α-helix	255-259	5
β-strand	265-267	3	3
α-helix	278-282	5
β-strand	288-290	3	3
α-helix	301-305	5
β-strand	311-313	3	4
α-helix	326-329	4
β-strand	335-337	3	4
α-helix	346-347	2
α-helix	351-354	4
β-strand	359-361	3	4
α-helix	370-371	2
β-strand	383-385	3	4
α-helix	398-400	3
β-strand	406-408	3	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	465-469	5
β-strand	475-477	3	4
α-helix	488-492	5
β-strand	498-500	3	4
α-helix	511-515	5
β-strand	521-523	3	4
α-helix	535-539	5
β-strand	545-547	3	4
α-helix	558-563	6
α-helix	565-575	11

Chain C: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-18	10
α-helix	23	1
α-helix	32-48	17
β-strand	52-55	4	5
β-strand	59-62	4	6
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	169-171	3	5
α-helix	184-187	4
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	7
β-strand	216-218	3	7
β-strand	225-227	3	7
α-helix	229-238	10
β-strand	243-246	4	5
β-strand	253	1	8
β-strand	255-258	4	5
β-strand	263-266	4	5
β-strand	279	1	8
β-strand	280-285	6	6
β-strand	291-296	6	6

Chain D: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	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	152-155	4	9
β-strand	156	1	10
α-helix	161	1
β-strand	162	1	10
α-helix	164-177	14

Chain E: 23 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	88-100	13
β-strand	104-106	3	11
α-helix	117-121	5
β-strand	127-129	3	11
α-helix	140-144	5
β-strand	150-152	3	11
α-helix	163-167	5
β-strand	173-175	3	11
α-helix	188-190	3
β-strand	196-198	3	11
α-helix	209-213	5
β-strand	219-221	3	11
α-helix	232-236	5
β-strand	242-244	3	11
α-helix	255-259	5
β-strand	265-267	3	11
α-helix	278-282	5
β-strand	288-290	3	11
α-helix	301-305	5
β-strand	311-313	3	12
α-helix	326-329	4
β-strand	335-337	3	12
α-helix	346-347	2
α-helix	351-354	4
β-strand	359-361	3	12
α-helix	370-371	2
β-strand	383-385	3	12
α-helix	398-400	3
β-strand	406-408	3	12
α-helix	419-423	5
β-strand	429-431	3	12
α-helix	442-446	5
β-strand	452-454	3	12
α-helix	465-469	5
β-strand	475-477	3	12
α-helix	488-492	5
β-strand	498-500	3	12
α-helix	511-515	5
β-strand	521-523	3	12
α-helix	535-539	5
β-strand	545-547	3	12
α-helix	558-561	4
α-helix	565-575	11

Chain F: 13 helices, 17 β-strands

Element	Residues	Length	Sheet
α-helix	9-18	10
α-helix	32-47	16
β-strand	52-55	4	13
β-strand	59-62	4	6
β-strand	64	1	14
α-helix	69-79	11
β-strand	87-89	3	6
α-helix	100-113	14
β-strand	118-120	3	6
α-helix	121-123	3
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	13
β-strand	169-171	3	13
α-helix	183-187	5
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	15
β-strand	216-218	3	15
β-strand	225-227	3	15
α-helix	229-238	10
β-strand	243-246	4	13
β-strand	253-254	2	6
β-strand	255-258	4	13
β-strand	263-266	4	13
β-strand	267	1	14
α-helix	272-274	3
β-strand	279-285	7	6
β-strand	291-296	6	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ras-related protein M-Ras	A, D	protein	180	Homo sapiens	O14807 (AlphaFold model)
Leucine-rich repeat protein SHOC-2	B, E	protein	505	Homo sapiens	Q9UQ13 (AlphaFold model)
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	C, F	protein	297	Homo sapiens	P62136 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>7TXH_1 Ras-related protein M-Ras (chains A, D)
GPMATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDN
QWAILDVLDTAGREEFSAMREQYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRES
FPMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQ

Sequence of entity 2 (B, E), FASTA

>7TXH_2 Leucine-rich repeat protein SHOC-2 (chains B, E)
GPGTRKKSSNAEVIKELNKCREENSMRLDLSKRSIHILPSSIKELTQLTELYLYSNKLQS
LPAEVGCLVNLMTLALSENSLTSLPDSLDNLKKLRILDLRHNKLREIPSVVYRLDSLTTL
YLRFNRITTVEKDIKNLSKLSMLSIRENKIKQLPAEIGELCNLITLDVAHNQLEHLPKEI
GNCTQITNLDLQHNELLDLPDTIGNLSSLSRLGLRYNRLSAIPRSLAKCSALEELNLENN
NISTLPESLLSSLVKLNSLTLARNCFQLYPVGGPSQFSTIYSLNMEHNRINKIPFGIFSR
AKVLSKLNMKDNQLTSLPLDFGTWTSMVELNLATNQLTKIPEDVSGLVSLEVLILSNNLL
KKLPHGLGNLRKLRELDLEENKLESLPNEIAYLKDLQKLVLTNNQLTTLPRGIGHLTNLT
HLGLGENLLTHLPEEIGTLENLEELYLNDNPNLHSLPFELALCSKLSIMSIENCPLSHLP
PQIVAGGPSFIIQFLKMQGPYRAMV

Sequence of entity 3 (C, F), FASTA

>7TXH_3 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains C, F)
SNALNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICG
DIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRG
NHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSM
EQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDLDL
ICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD

Ligands and cofactors

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

Water and common crystallization additives (GOL) are not listed.

Primary citation

Structure of the MRAS-SHOC2-PP1C phosphatase complex. Hauseman, Z.J., Fodor, M., Dhembi, A. et al. Nature (2022) 609:416-423. DOI 10.1038/s41586-022-05086-1 · PubMed

Other PDB entries of the same protein (UniProt O14807 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9O0P 1.5 Å, Crystal structure of GDP-bound mutant MRAS in complex with MRTX1133
9O0Q 1.9 Å, Crystal structure of GMPPNP-bound mutant MRAS in complex with MRTX1133
9C1A 1.96 Å, Crystal structure of GDP-bound human M-RAS protein in crystal form I
9B4R 2.1 Å, Crystal structure of MRAS bound to GMPPNP
7TVF 2.17 Å, Crystal structure of the SHOC2-MRAS-PP1CA (SMP) complex to a resolution of 2.17 Angstrom
9C1B 2.27 Å, Crystal structure of GDP-bound human M-RAS protein in crystal form II
9B4T 2.75 Å, Crystal structure of the MRAS-p110alpha complex
9MEZ 2.8 Å, Crystal structure of MRAS(GDP) bound to LZTR1(Kelch domain)
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

Browse structure collections

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