Crystal structure of NRas-G12D in complex with GDP and compound 1. Determined by X-ray diffraction at 1.8 Å resolution. Released 25 Feb 2026.
Explore 9Y0G in 3D Show helices and sheets RCSB PDB PDBe
9Y0G contains 12 α-helices and 12 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-9 | 8 | 1 |
| α-helix | 16-25 | 10 | |
| β-strand | 37-46 | 10 | 1 |
| β-strand | 49-57 | 9 | 1 |
| α-helix | 66-73 | 8 | |
| β-strand | 77-83 | 7 | 1 |
| α-helix | 87-91 | 5 | |
| α-helix | 93-104 | 12 | |
| β-strand | 111-116 | 6 | 1 |
| α-helix | 127-137 | 11 | |
| β-strand | 141-143 | 3 | 1 |
| α-helix | 152-166 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-10 | 9 | 1 |
| α-helix | 16-25 | 10 | |
| β-strand | 37-46 | 10 | 1 |
| β-strand | 49-57 | 9 | 1 |
| α-helix | 69-74 | 6 | |
| β-strand | 77-83 | 7 | 1 |
| α-helix | 87-91 | 5 | |
| α-helix | 93-104 | 12 | |
| β-strand | 111-116 | 6 | 1 |
| α-helix | 127-137 | 11 | |
| β-strand | 141-143 | 3 | 1 |
| α-helix | 152-167 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTPase NRas | A, B | protein | 171 | Homo sapiens | P01111 (AlphaFold model) |
>9Y0G_1 GTPase NRas (chains A, B) GPMTEYKLVVVGADGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDT AGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDVPMVLVGNKS DLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMK
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
| A1CRR | (5P)-3-chloro-4-cyclopropyl-5-(4-[(1R,5S)-3,8-diazabicyclo[3.2.1]octan-3-yl]-8-… | C30 H34 Cl F N6 O2 | 1 |
| MG | Magnesium ion | Mg | 3 |
| CIT | Citric acid | C6 H8 O7 | 1 |
Structure-Guided Development of NRAS G12D Inhibitors Based on a 5‐Azaindole Core. Cox, J.B., Nair, V., Mandal, P. et al. ACS Med Chem Lett (2026) 17:425-432. DOI 10.1021/acsmedchemlett.5c00647 · PubMed
Other PDB entries of the same protein (UniProt P01111 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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