4rsg

Neutron Diffraction
1.91Å resolution

Neutron crystal structure of Ras bound to the GTP analogue GppNHp

Released:

Function and Biology Details

Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-133956 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Spacegroup: P3221
Unit cell:
a: 40.084Å b: 40.084Å c: 160.785Å α: 90° β: 90° γ: 120°
R-values:
R R work R free 0.253 0.249 0.288
Expression system: Escherichia coli