› 1fot

X-ray diffraction
2.8Å resolution

STRUCTURE OF THE UNLIGANDED CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT FROM SACCHAROMYCES CEREVISIAE

Released:
DOI: 10.2210/pdb1fot/pdb
PDB entry 1fot coloured by chain, front view.
PDB entry 1fot coloured by chain, side view.
PDB entry 1fot coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure of the unliganded cAMP-dependent protein kinase catalytic subunit from Saccharomyces cerevisiae.
Mashhoon N, Carmel G, Pflugrath JW, Kuret J
Arch Biochem Biophys 387 11-9 (2001)
PMID: 11368172

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138981 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cAMP-dependent protein kinase type 1 Chain: A
Molecule details ›
Chain: A
Length: 318 amino acids
Theoretical weight: 37.41 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P06244 (Residues: 81-397; Coverage: 80%)
Gene names: J0541, PKA1, SRA3, TPK1, YJL164C
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P6522
Unit cell:
a: 61Å b: 61Å c: 322Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.194 0.194 0.243
Expression system: Saccharomyces cerevisiae

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Citations

1 review citation

Yeast Protein Kinase A Isoforms: A Means of Encoding Specificity in the Response to Diverse Stress Conditions?
Creamer et al. (2022)
4 other articles

5 mentions without citation

Reproducing crystal binding modes of ligand functional groups using Site-Identification by Ligand Competitive Saturation (SILCS) simulations.
Raman et al. (2011)
4 more