3k9n

X-ray diffraction
2Å resolution

Allosteric modulation of H-Ras GTPase

Released:
Source organism: Homo sapiens
Primary publication:
Allosteric modulation of Ras positions Q61 for a direct role in catalysis.
Proc Natl Acad Sci U S A 107 4931-6 (2010)
PMID: 20194776

Function and Biology Details

Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:

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: 18.86 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

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3121
Unit cell:
a: 38.423Å b: 38.423Å c: 191.749Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.214 0.277
Expression system: Escherichia coli