Structure analysis

STRUCTURE OF THE MAMMALIAN CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE AND AN INHIBITOR PEPTIDE DISPLAYS AN OPEN CONFORMATION

X-ray diffraction
2.9Å resolution
Source organisms:
Assembly composition:
hetero tetramer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
Download    3D Visualisation
Multimeric state: hetero tetramer
Accessible surface area: 29500 Å2
Buried surface area: 6100 Å2
Dissociation area: 950 Å2
Dissociation energy (ΔGdiss): -2 kcal/mol
Dissociation entropy (TΔSdiss): 14 kcal/mol
Interface energy (ΔGint): -17 kcal/mol
Symmetry number: 2

Macromolecules

Chain: E
Length: 350 amino acids
Theoretical weight: 40.62 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P36887 (Residues: 2-351; Coverage: 100%)
Gene name: PRKACA
Pfam: Protein kinase domain
InterPro:
CATH:
SCOP: Protein kinases, catalytic subunit

Search similar proteins

Chain: I
Length: 20 amino acids
Theoretical weight: 2.48 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P61926 (Residues: 6-25; Coverage: 26%)
Gene names: PKIA, PRKACN1
InterPro: cAMP-dependent protein kinase inhibitor

Search similar proteins