PDBe 2v55

X-ray diffraction
3.7Å resolution

Mechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure

Released:
Source organism: Homo sapiens

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Rho-associated protein kinase 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 406 amino acids
Theoretical weight: 47.02 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q13464 (Residues: 1-406; Coverage: 30%)
Gene name: ROCK1
Sequence domains: Protein kinase domain
Structure domains:
Rho-related GTP-binding protein RhoE Chains: B, D
Molecule details ›
Chains: B, D
Length: 200 amino acids
Theoretical weight: 22.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P61587 (Residues: 1-200; Coverage: 82%)
Gene names: ARHE, RHO8, RHOE, RND3
Sequence domains: Ras family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P6522
Unit cell:
a: 152.477Å b: 152.477Å c: 531.274Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.238 0.238 0.269
Expression systems:
  • Spodoptera frugiperda
  • Escherichia coli BL21(DE3)