› 1q21

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURES AT 2.2 ANGSTROMS RESOLUTION OF THE CATALYTIC DOMAINS OF NORMAL RAS PROTEIN AND AN ONCOGENIC MUTANT COMPLEXED WITH GSP

Released:
DOI: 10.2210/pdb1q21/pdb
PDB entry 1q21 coloured by chain, front view.
PDB entry 1q21 coloured by chain, side view.
PDB entry 1q21 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP.
Tong LA, de Vos AM, Milburn MV, Kim SH
J Mol Biol 217 503-16 (1991)
PMID: 1899707

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 Chain: A
Molecule details ›
Chain: A
Length: 171 amino acids
Theoretical weight: 19.52 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01112 (Residues: 1-171; Coverage: 91%)
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 GDP 1 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6522
Unit cell:
a: 83.2Å b: 83.2Å c: 105.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 not available
Expression system: Not provided

Quick links

Citations

25 review citations

RAS oncogenes: the first 30 years.
Malumbres et al. (2003)
24 more

412 mentions without citation

Recent advances in neuroblastoma.
Maris JM. (2010)
411 more