9O0P: GDP-bound mutant MRAS

Crystal structure of GDP-bound mutant MRAS in complex with MRTX1133. Determined by X-ray diffraction at 1.5 Å resolution. Released 21 Jan 2026.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,304
Mol. weight: 43.09 kDa
Ligands: GDP, MG, 6IC
Released: 21 Jan 2026

Explore 9O0P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9O0P contains 19 α-helices and 16 β-strands across 2 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	13-19	7	1
α-helix	26-33	8
α-helix	39-41	3
β-strand	47-56	10	1
β-strand	59-67	9	1
α-helix	76-83	8
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	138-147	10
β-strand	152-154	3	1
β-strand	156	1	2
α-helix	161	1
β-strand	162	1	2
α-helix	164-176	13

Chain B: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	13-19	7	1
α-helix	26-33	8
α-helix	39-41	3
β-strand	48-56	9	1
β-strand	59-67	9	1
α-helix	71-72	2
α-helix	78-82	5
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	138-147	10
β-strand	152-154	3	1
β-strand	156	1	3
α-helix	161	1
β-strand	162	1	3
α-helix	164-176	13

Molecules and chains

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

Sequence of entity 1 (A, B), FASTA

>9O0P_1 Ras-related protein M-Ras (chains A, B)
GMATSAVPSDNLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQ
WAILDVLDTAGQEEYSAMREQYMRTGDGFLIVYSVTDKASFEHVDHYHQQILRVKDRESF
PMILVANKVDLMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQ

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
MG	Magnesium ion	Mg	1
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	2

Water and common crystallization additives (CL) 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:

9O0Q 1.9 Å, Crystal structure of GMPPNP-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

About this viewer

MolViewer shows 9O0P directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.