PDBe 1zw6

X-ray diffraction
1.5Å resolution

Crystal Structure of the GTP-bound form of RasQ61G

Released:
Source organism: Homo sapiens
Primary publication:
Structure of a transient intermediate for GTP hydrolysis by ras.
Structure 14 427-36 (2006)
PMID: 16531227

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (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: 18.82 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:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: R32
Unit cell:
a: 88.776Å b: 88.776Å c: 134.392Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.146 0.144 0.174
Expression system: Escherichia coli