8FMI: Human KRAS

Crystal structure of human KRAS at 1.12 A. Determined by X-ray diffraction at 1.12 Å resolution. Released 29 Nov 2023.

Method
X-ray diffraction
Resolution
1.12 Å
Organism
Homo sapiens
Chains
1
Atoms
1,717
Mol. weight
19.78 kDa
Ligands
MG, GDP
Released
29 Nov 2023

Explore 8FMI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8FMI contains 5 α-helices and 6 β-strands across 1 chain. 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: 5 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand3-971
α-helix16-2510
β-strand38-4691
β-strand49-5791
α-helix65-7410
β-strand77-8371
α-helix87-10418
β-strand111-11661
α-helix127-13711
β-strand141-14331
α-helix152-16716

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Isoform 2B of GTPase KRasAprotein170Homo sapiensP01116 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8FMI_1 Isoform 2B of GTPase KRas (chains A)
GMTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTA
GQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSD
LPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEK

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21

Primary citation

Crystal Packing Reveals a Potential Autoinhibited KRAS Dimer Interface and a Strategy for Small-Molecule Inhibition of RAS Signaling. Brenner, R.J., Landgraf, A.D., Bum-Erdene, K. et al. Biochemistry (2023) 62:3206-3213. DOI 10.1021/acs.biochem.3c00378 · PubMed

Other PDB entries of the same protein (UniProt P01116 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 8FMI 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.