8TVK: KRAS 1-169 G12C Mutant at 100k

KRAS 1-169 G12C Mutant at 100k. Determined by X-ray diffraction at 1.04 Å resolution. Released 28 Aug 2024.

Method
X-ray diffraction
Resolution
1.04 Å
Organism
Homo sapiens
Chains
1
Atoms
1,628
Mol. weight
19.79 kDa
Ligands
MG, GDP
Released
28 Aug 2024

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

Secondary structure: helices and β-sheets

8TVK 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 KRasAprotein169Homo sapiensP01116 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8TVK_1 Isoform 2B of GTPase KRas (chains A)
MTEYKLVVVGACGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDL
PSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEK

Ligands and cofactors

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

Primary citation

Revealing Functional Hotspots: Temperature-Dependent Crystallography of K-RAS Highlights Allosteric and Druggable Sites. Deck, S.L., Xu, M., Milano, S.K. et al. bioRxiv (2025). DOI 10.1101/2025.02.27.639303 · PubMed

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

Browse structure collections

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