› 3a8x

X-ray diffraction
2Å resolution

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-154422 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein kinase C iota type Chains: A, B
Molecule details ›
Chains: A, B
Length: 345 amino acids
Theoretical weight: 39.85 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P41743 (Residues: 249-588; Coverage: 57%)
Gene names: DXS1179E, PRKCI
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
1 modified residue:
Ligand TPO 4 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: C2221
Unit cell:
a: 84.896Å b: 89.153Å c: 204.265Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.223 0.271
Expression system: Spodoptera frugiperda

Quick links

Citations

4 review citations

AGC protein kinases: from structural mechanism of regulation to allosteric drug development for the treatment of human diseases.
Arencibia et al. (2013)
3 more

11 mentions without citation

Design principles underpinning the regulatory diversity of protein kinases.
Oruganty et al. (2012)
10 more