PDBe 1cmk

X-ray diffraction
2.9Å resolution

CRYSTAL STRUCTURES OF THE MYRISTYLATED CATALYTIC SUBUNIT OF CAMP-DEPENDENT PROTEIN KINASE REVEAL OPEN AND CLOSED CONFORMATIONS

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero 12-mer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
cAMP-dependent protein kinase catalytic subunit alpha Chain: E
Molecule details ›
Chain: E
Length: 350 amino acids
Theoretical weight: 40.71 KDa
Source organism: Sus scrofa
Expression system: Not provided
UniProt:
  • Canonical: P36887 (Residues: 2-351; Coverage: 100%)
Gene name: PRKACA
Sequence domains: Protein kinase domain
Structure domains:
cAMP-dependent protein kinase inhibitor alpha Chain: I
Molecule details ›
Chain: I
Length: 22 amino acids
Theoretical weight: 2.45 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P61925 (Residues: 6-27; Coverage: 29%)
Gene names: PKIA, PRKACN1

Ligands and Environments

2 bound ligands:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P4132
Unit cell:
a: 171.52Å b: 171.52Å c: 171.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 not available
Expression system: Not provided