› 1kmq

X-ray diffraction
1.55Å resolution

Crystal Structure of a Constitutively Activated RhoA Mutant (Q63L)

Released:
DOI: 10.2210/pdb1kmq/pdb
PDB entry 1kmq coloured by chain, front view.
PDB entry 1kmq coloured by chain, side view.
PDB entry 1kmq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a constitutively activated RhoA mutant (Q63L) at 1.55 A resolution.
Longenecker K, Read P, Lin SK, Somlyo AP, Nakamoto RK, Derewenda ZS
Acta Crystallogr D Biol Crystallogr 59 876-80 (2003)
PMID: 12777804

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-158275 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transforming protein RhoA Chain: A
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 20.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P61586 (Residues: 4-181; Coverage: 92%)
Gene names: ARH12, ARHA, RHO12, RHOA
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P21212
Unit cell:
a: 60.581Å b: 73.34Å c: 48.041Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.19
Expression system: Escherichia coli

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Citations

1 review citation

Ca2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated by G proteins, kinases, and myosin phosphatase.
Somlyo et al. (2003)
13 other articles

9 mentions without citation

Predicting new indications for approved drugs using a proteochemometric method.
Dakshanamurthy et al. (2012)
8 more