› 5p21

X-ray diffraction
1.35Å resolution

REFINED CRYSTAL STRUCTURE OF THE TRIPHOSPHATE CONFORMATION OF H-RAS P21 AT 1.35 ANGSTROMS RESOLUTION: IMPLICATIONS FOR THE MECHANISM OF GTP HYDROLYSIS

Released:
DOI: 10.2210/pdb5p21/pdb
PDB entry 5p21 coloured by chain, front view.
PDB entry 5p21 coloured by chain, side view.
PDB entry 5p21 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis.
Pai EF, Krengel U, Petsko GA, Goody RS, Kabsch W, Wittinghofer A
EMBO J 9 2351-9 (1990)
PMID: 2196171

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133977 (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: Not provided
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

2 bound ligands:
Ligand MG 1 x MG
Ligand GNP 1 x GNP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 40.3Å b: 40.3Å c: 162.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 not available
Expression system: Not provided

Quick links

Citations

88 review citations

The GTPase superfamily: conserved structure and molecular mechanism.
Bourne et al. (1991)
87 more

148 mentions without citation

Ras oncogenes: split personalities.
Karnoub et al. (2008)
147 more