PDBe 1syk

X-ray diffraction
2.8Å resolution

Crystal structure of E230Q mutant of cAMP-dependent protein kinase reveals unexpected apoenzyme conformation

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cAMP-dependent protein kinase catalytic subunit alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 350 amino acids
Theoretical weight: 40.66 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P05132 (Residues: 2-351; Coverage: 100%)
Gene names: Pkaca, Prkaca
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands

2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P42
Unit cell:
a: 120.3Å b: 120.3Å c: 58.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.249
Expression system: Escherichia coli