9O0Q: GMPPNP-bound mutant MRAS

Crystal structure of GMPPNP-bound mutant MRAS in complex with MRTX1133. Determined by X-ray diffraction at 1.9 Å resolution. Released 21 Jan 2026.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 3
Atoms: 4,877
Mol. weight: 66.35 kDa
Ligands: 6IC, MG, GNP
Released: 21 Jan 2026

Explore 9O0Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9O0Q contains 24 α-helices and 24 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: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	1
α-helix	26-35	10
β-strand	48-56	9	1
β-strand	59-67	9	1
α-helix	76-82	7
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	152-154	3	1
β-strand	156	1	2
α-helix	161	1
β-strand	162	1	2
α-helix	164-177	14

Chain B: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	3
α-helix	26-35	10
β-strand	48-56	9	3
β-strand	59-67	9	3
α-helix	76-83	8
β-strand	87-93	7	3
α-helix	97-101	5
α-helix	103-114	12
β-strand	121-126	6	3
α-helix	131-133	3
α-helix	138-147	10
β-strand	152-154	3	3
β-strand	156	1	4
α-helix	161	1
β-strand	162	1	4
α-helix	164-177	14

Chain C: 8 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	3
α-helix	26-35	10
β-strand	48-56	9	3
β-strand	59-67	9	3
α-helix	76-83	8
β-strand	87-93	7	3
α-helix	97-101	5
α-helix	103-114	12
β-strand	121-126	6	3
α-helix	131-133	3
α-helix	138-148	11
β-strand	152-154	3	3
β-strand	156	1	5
α-helix	161	1
β-strand	162	1	5
α-helix	164-177	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ras-related protein M-Ras	A, B, C	protein	179	Homo sapiens	O14807 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>9O0Q_1 Ras-related protein M-Ras (chains A, B, C)
GMATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQ
WAILDVLDTAGQEEYSAMREQYMRTGDGFLIVYSVTDKASFEHVDHYHQQILRVKDRESF
PMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQ

Ligands and cofactors

ID	Name	Formula	Copies
6IC	4-(4-[(1R,5S)-3,8-diazabicyclo[3.2.1]octan-3-yl]-8-fluoro-2-{[(2R,4R,7aS)-2-flu…	C33 H31 F3 N6 O2	3
MG	Magnesium ion	Mg	3
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	3

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

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 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
7TXH 1.95 Å, Human MRas Q71R in complex with human Shoc2 LRR domain M173I and human PP1Ca
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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