› 4dlt

X-ray diffraction
1.7Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-133956 (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: 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: R32
Unit cell:
a: 88.704Å b: 88.704Å c: 134.36Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.181 0.204
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Drugging Ras GTPase: a comprehensive mechanistic and signaling structural view.
Lu et al. (2016)
4 more

2 mentions without citation

A structural model of a Ras-Raf signalosome.
Mysore et al. (2021)
1 more