› 5e95

X-ray diffraction
1.4Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133962 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mb(NS1) Chain: B
Molecule details ›
Chain: B
Length: 97 amino acids
Theoretical weight: 10.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
Structure domains: Immunoglobulins
GTPase HRas, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 168 amino acids
Theoretical weight: 19.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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 GDP 1 x GDP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P1
Unit cell:
a: 35.897Å b: 36.276Å c: 54.348Å
α: 86.3° β: 74.23° γ: 85.2°
R-values:
R R work R free
0.164 0.163 0.192
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

51 review citations

RAS Proteins and Their Regulators in Human Disease.
Simanshu et al. (2017)
50 more

20 mentions without citation

RAS-targeted therapies: is the undruggable drugged?
Moore et al. (2020)
19 more