› 1cdk

X-ray diffraction
2Å resolution

CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT (E.C.2.7.1.37) (PROTEIN KINASE A) COMPLEXED WITH PROTEIN KINASE INHIBITOR PEPTIDE FRAGMENT 5-24 (PKI(5-24) ISOELECTRIC VARIANT CA) AND MN2+ ADENYLYL IMIDODIPHOSPHATE (MNAMP-PNP) AT PH 5.6 AND 7C AND 4C

Released:
DOI: 10.2210/pdb1cdk/pdb
PDB entry 1cdk coloured by chain, front view.
PDB entry 1cdk coloured by chain, side view.
PDB entry 1cdk coloured by chain, top view.
Source organisms:
Primary publication:
Phosphotransferase and substrate binding mechanism of the cAMP-dependent protein kinase catalytic subunit from porcine heart as deduced from the 2.0 A structure of the complex with Mn2+ adenylyl imidodiphosphate and inhibitor peptide PKI(5-24).
Bossemeyer D, Engh RA, Kinzel V, Ponstingl H, Huber R
EMBO J 12 849-59 (1993)
PMID: 8384554

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153239 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
cAMP-dependent protein kinase catalytic subunit alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 350 amino acids
Theoretical weight: 40.63 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P36887 (Residues: 2-351; Coverage: 100%)
Gene name: PRKACA
Sequence domains: Protein kinase domain
Structure domains:
cAMP-dependent protein kinase inhibitor alpha Chains: I, J
Molecule details ›
Chains: I, J
Length: 20 amino acids
Theoretical weight: 2.23 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P61926 (Residues: 6-25; Coverage: 26%)
Gene names: PKIA, PRKACN1

Ligands and Environments

3 bound ligands:
Ligand MN 4 x MN
Ligand ANP 2 x ANP
Ligand MYR 2 x MYR
1 modified residue:
Ligand TPO 2 x TPO

Experiments and Validation Details

Entry percentile scores
Unit cell:
a: 107.61Å b: 80.6Å c: 110.1Å
α: 90° β: 88.59° γ: 90°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Not provided

Quick links

Citations

49 review citations

The conformational plasticity of protein kinases.
Huse et al. (2002)
48 more

35 mentions without citation

Substrate and docking interactions in serine/threonine protein kinases.
Goldsmith et al. (2007)
34 more