Crystal structure of N-acetylated KRAS (2-169) bound to GDP and Mg. Determined by X-ray diffraction at 1.01 Å resolution. Released 31 Jul 2019.
Explore 6P0Z in 3D Show helices and sheets RCSB PDB PDBe
6P0Z contains 10 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 | 3-9 | 7 | 1 |
| α-helix | 16-25 | 10 | |
| β-strand | 38-46 | 9 | 1 |
| β-strand | 49-57 | 9 | 1 |
| α-helix | 65-74 | 10 | |
| β-strand | 77-83 | 7 | 1 |
| α-helix | 87-104 | 18 | |
| 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 KRas | A, B | protein | 168 | Homo sapiens | P01116 (AlphaFold model) |
>6P0Z_1 GTPase KRas (chains A, B) TEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQ EEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLP SRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 2 |
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
| ACE | Acetyl group | C2 H4 O | 2 |
Water and common crystallization additives (PEG) are not listed.
Structures of N-terminally processed KRAS provide insight into the role of N-acetylation. Dharmaiah, S., Tran, T.H., Messing, S. et al. Sci Rep (2019) 9:10512-10512. DOI 10.1038/s41598-019-46846-w · PubMed
Other PDB entries of the same protein (UniProt P01116 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6P0Z 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.