› 221p

X-ray diffraction
2.3Å resolution

THREE-DIMENSIONAL STRUCTURES OF H-RAS P21 MUTANTS: MOLECULAR BASIS FOR THEIR INABILITY TO FUNCTION AS SIGNAL SWITCH MOLECULES

Released:
DOI: 10.2210/pdb221p/pdb
PDB entry 221p coloured by chain, front view.
PDB entry 221p coloured by chain, side view.
PDB entry 221p coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Three-dimensional structures of H-ras p21 mutants: molecular basis for their inability to function as signal switch molecules.
Krengel U, Schlichting I, Scherer A, Schumann R, Frech M, John J, Kabsch W, Pai EF, Wittinghofer A
Cell 62 539-48 (1990)
PMID: 2199064

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: 18.89 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
0.183 0.183 not available
Expression system: Not provided

Quick links

Citations

46 review citations

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

1 mention without citation

The role of conserved waters in conformational transitions of Q61H K-ras.
Prakash et al. (2012)