6P0Z: N-acetylated KRAS

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.

Method
X-ray diffraction
Resolution
1.01 Å
Organism
Homo sapiens
Chains
2
Atoms
3,395
Mol. weight
39.41 kDa
Ligands
MG, GDP, ACE
Released
31 Jul 2019

Explore 6P0Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A and B: 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
GTPase KRasA, Bprotein168Homo sapiensP01116 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6P0Z_1 GTPase KRas (chains A, B)
TEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQ
EEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLP
SRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTLVREIRKHKEK

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22
ACEAcetyl groupC2 H4 O2

Water and common crystallization additives (PEG) are not listed.

Primary citation

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:

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