3kud

X-ray diffraction
2.15Å resolution

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: 81 amino acids
Theoretical weight: 9.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04049 (Residues: 51-131; Coverage: 13%)
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: SLS BEAMLINE X10SA
Spacegroup: R32
Unit cell:
a: 91.13Å b: 91.13Å c: 277.98Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.238 0.237 0.264
Expression system: Escherichia coli