PDBe 4g3x

X-ray diffraction
3.25Å resolution

Crystal Structure of Q61L H-Ras-GppNHp bound to the RBD of Raf Kinase

Released:
Source organism: Homo sapiens

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
GTPase HRas, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.86 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P01112 (Residues: 1-166; Coverage: 88%)
Gene names: HRAS, HRAS1
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases
RAF proto-oncogene serine/threonine-protein kinase Chain: B
Molecule details ›
Chain: B
Length: 77 amino acids
Theoretical weight: 8.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P04049 (Residues: 55-131; Coverage: 12%)
Gene names: RAF, RAF1
Sequence domains: Raf-like Ras-binding domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P321
Unit cell:
a: 91.4Å b: 91.4Å c: 93.11Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.275 0.25 0.271
Expression system: Escherichia coli