Crystal structure of GDP-bound NRAS with ten residues long internal tandem duplication in the switch II region. Determined by X-ray diffraction at 1.65 Å resolution. Released 20 May 2020.
Explore 6WGH in 3D Show helices and sheets RCSB PDB PDBe
6WGH contains 11 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 | 2-10 | 9 | 1 |
| α-helix | 16-25 | 10 | |
| β-strand | 37-46 | 10 | 1 |
| β-strand | 49-57 | 9 | 1 |
| α-helix | 76-84 | 9 | |
| β-strand | 87-93 | 7 | 1 |
| α-helix | 97-114 | 18 | |
| β-strand | 121-126 | 6 | 1 |
| α-helix | 137-147 | 11 | |
| β-strand | 151-153 | 3 | 1 |
| α-helix | 162-177 | 16 |
| 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 | 80-84 | 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 | 137-147 | 11 | |
| β-strand | 151-153 | 3 | 1 |
| α-helix | 162-176 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GTPase NRas | A, B | protein | 181 | Homo sapiens | P01111 (AlphaFold model) |
>6WGH_1 GTPase NRas (chains A, B) GMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTA GQEEYILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNSKSFADINLYREQIKRVKDSDDV PMVLVGNKCDLPTRTVDTKQAHELAKSYGIPFIETSAKTRQGVEDAFYTLVREIRQYRMK K
| ID | Name | Formula | Copies |
|---|---|---|---|
| FLC | Citrate anion | C6 H5 O7 | 1 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
| MG | Magnesium ion | Mg | 3 |
Water and common crystallization additives (GOL) are not listed.
RASinternal tandem duplication disrupts GTPase-activating protein (GAP) binding to activate oncogenic signaling. Nelson, A.C., Turbyville, T.J., Dharmaiah, S. et al. J Biol Chem (2020) 295:9335-9348. DOI 10.1074/jbc.RA119.011080 · 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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