› 2f2u

X-ray diffraction
2.4Å resolution

crystal structure of the Rho-kinase kinase domain

Released:
DOI: 10.2210/pdb2f2u/pdb
PDB entry 2f2u coloured by chain, front view.
PDB entry 2f2u coloured by chain, side view.
PDB entry 2f2u coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Molecular mechanism for the regulation of rho-kinase by dimerization and its inhibition by fasudil.
Yamaguchi H, Kasa M, Amano M, Kaibuchi K, Hakoshima T
Structure 14 589-600 (2006)
PMID: 16531242

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173301 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rho-associated protein kinase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 402 amino acids
Theoretical weight: 45.78 KDa
Source organism: Bos taurus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q28021 (Residues: 18-417; Coverage: 29%)
Gene name: ROCK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand M77 2 x M77
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P41212
Unit cell:
a: 102.531Å b: 102.531Å c: 257.185Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.235
Expression system: Spodoptera frugiperda

Quick links

Citations

22 review citations

Rho-kinase/ROCK: A key regulator of the cytoskeleton and cell polarity.
Amano et al. (2010)
21 more

10 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
9 more