› 8g47

Electron Microscopy
3.19Å resolution

KRAS G12C complex with GDP and AMG 510 imaged on a cryo-EM imaging scaffold

Released:
DOI: 10.2210/pdb8g47/pdb
PDB entry 8g47 coloured by chain, front view.
PDB entry 8g47 coloured by chain, side view.
PDB entry 8g47 coloured by chain, top view.
Source organisms:
Primary publication:
Cryo-EM structure determination of small therapeutic protein targets at 3 Å-resolution using a rigid imaging scaffold.
Castells-Graells R, Meador K, Arbing MA, Sawaya MR, Gee M, Cascio D, Gleave E, Debreczeni JÉ, Breed J, Leopold K, Patel A, Jahagirdar D, Lyons B, Subramaniam S, Phillips C, Yeates TO
OpenAccess logo Proc Natl Acad Sci U S A 120 e2305494120 (2023)
PMID: 37669364
Related structures: EMD-29715

Function and Biology Details

Reaction catalysed: 
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-272016 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RCG-33 - Cryo-EM imaging scaffold subunit B fused to DARPin Chain: A
Molecule details ›
Chain: A
Length: 321 amino acids
Theoretical weight: 35.45 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
GTPase KRas, N-terminally processed Chain: B
Molecule details ›
Chain: B
Length: 189 amino acids
Theoretical weight: 21.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01116 (Residues: 1-169; Coverage: 89%)
  • Best match: P01116-2 (Residues: 1-169)
Gene names: KRAS, KRAS2, RASK2
Sequence domains: Ras family

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand GDP 1 x GDP
Ligand MOV 1 x MOV
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.19Å
Relevant EMDB volumes: EMD-29715
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Applications and prospects of cryo-EM in drug discovery.
Zhu et al. (2023)
1 more