4TQA: GTPase KRas

Crystal Structure of a GDP-bound G13D Oncogenic Mutant of Human GTPase KRas. Determined by X-ray diffraction at 1.13 Å resolution. Released 10 Jun 2015.

Method
X-ray diffraction
Resolution
1.13 Å
Organism
Homo sapiens
Chains
2
Atoms
3,188
Mol. weight
39.45 kDa
Ligands
MG, GDP
Released
10 Jun 2015

Explore 4TQA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4TQA 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.

Chains A and B: 5 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand2-981
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
GTPase KRasA, Bprotein169Homo sapiensP01116 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4TQA_1 GTPase KRas (chains A, B)
GMTEYKLVVVGAGDVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTA
GQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCD
LPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKE

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22

Primary citation

Biochemical and Structural Analysis of Common Cancer-Associated KRAS Mutations. Hunter, J.C., Manandhar, A., Carrasco, M.A. et al. Mol Cancer Res (2015) 13:1325-1335. DOI 10.1158/1541-7786.MCR-15-0203 · 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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