› 2uzv

X-ray diffraction
2.5Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132597 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
cAMP-dependent protein kinase inhibitor alpha Chain: 2
Molecule details ›
Chain: 2
Length: 20 amino acids
Theoretical weight: 2.23 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: Q3SX13 (Residues: 6-25; Coverage: 26%)
Gene name: PKIA
cAMP-dependent protein kinase catalytic subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 336 amino acids
Theoretical weight: 39.22 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00517 (Residues: 16-351; Coverage: 96%)
Gene name: PRKACA
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SS5 1 x SS5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 72.755Å b: 74.748Å c: 80.049Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.251 0.251 0.316
Expression systems:
  • Not provided
  • Escherichia coli

Quick links

Citations

3 review citations

Novel inhibitors of AKT: assessment of a different approach targeting the pleckstrin homology domain.
Meuillet EJ. (2011)
2 more

1 mention without citation

Binding of protein kinase inhibitors to synapsin I inferred from pair-wise binding site similarity measurements.
Defranchi et al. (2010)