Structure analysis

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

X-ray diffraction
2.8Å resolution
Source organism: Mus musculus
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 17650.41 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138536
Assembly 2
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Multimeric state: monomeric
Accessible surface area: 15760.43 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-138536

Macromolecules

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
Pfam: Protein kinase domain
InterPro:
CATH:

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