4g0n

X-ray diffraction
2.45Å resolution

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

Released:
Source organism: Homo sapiens

Function and Biology Details

Reactions catalysed:
GTP + H(2)O = GDP + phosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-133958 (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: 18.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: 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: 78 amino acids
Theoretical weight: 8.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04049 (Residues: 54-131; 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

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P321
Unit cell:
a: 90.44Å b: 90.44Å c: 92.703Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.186 0.181 0.229
Expression system: Escherichia coli