› 1iaq

X-ray diffraction
2.9Å resolution

C-H-RAS P21 PROTEIN MUTANT WITH THR 35 REPLACED BY SER (T35S) COMPLEXED WITH GUANOSINE-5'-[B,G-IMIDO] TRIPHOSPHATE

Released:
DOI: 10.2210/pdb1iaq/pdb
PDB entry 1iaq coloured by chain, front view.
PDB entry 1iaq coloured by chain, side view.
PDB entry 1iaq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Dynamic properties of the Ras switch I region and its importance for binding to effectors.
Spoerner M, Herrmann C, Vetter IR, Kalbitzer HR, Wittinghofer A
Proc Natl Acad Sci U S A 98 4944-9 (2001)
PMID: 11320243

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133956 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GTPase HRas, N-terminally processed Chains: A, B, C
Molecule details ›
Chains: A, B, C
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

2 bound ligands:
Ligand MG 3 x MG
Ligand GNP 3 x GNP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571, null
Spacegroup: P212121
Unit cell:
a: 63.89Å b: 79.06Å c: 94.04Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.242 0.282
Expression system: Escherichia coli

Quick links

Citations

25 review citations

Structure-function relationships of the G domain, a canonical switch motif.
Wittinghofer et al. (2011)
24 more

4 mentions without citation

Dynamic properties of the Ras switch I region and its importance for binding to effectors.
Spoerner et al. (2001)
3 more