› 1ctq

X-ray diffraction
1.26Å resolution

STRUCTURE OF P21RAS IN COMPLEX WITH GPPNHP AT 100 K

Released:
DOI: 10.2210/pdb1ctq/pdb
PDB entry 1ctq coloured by chain, front view.
PDB entry 1ctq coloured by chain, side view.
PDB entry 1ctq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins.
Scheidig AJ, Burmester C, Goody RS
Structure 7 1311-24 (1999)
PMID: 10574788

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 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P3221
Unit cell:
a: 39.67Å b: 39.67Å c: 158.409Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.172 0.224
Expression system: Escherichia coli

Quick links

Citations

24 review citations

RAS oncogenes: weaving a tumorigenic web.
Pylayeva-Gupta et al. (2011)
23 more

39 mentions without citation

The proteome: structure, function and evolution.
Fleming et al. (2006)
38 more