› 1rdq

X-ray diffraction
1.26Å resolution

Hydrolysis of ATP in the crystal of Y204A mutant of cAMP-dependent protein kinase

Released:
DOI: 10.2210/pdb1rdq/pdb
PDB entry 1rdq coloured by chain, front view.
PDB entry 1rdq coloured by chain, side view.
PDB entry 1rdq coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of a cAMP-dependent protein kinase mutant at 1.26A: new insights into the catalytic mechanism.
Yang J, Ten Eyck LF, Xuong NH, Taylor SS
J Mol Biol 336 473-87 (2004)
PMID: 14757059

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-138548 (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: 40.57 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P05132 (Residues: 2-351; Coverage: 100%)
Gene names: Pkaca, Prkaca
Sequence domains: Protein kinase domain
Structure domains:
cAMP-dependent protein kinase inhibitor, alpha form Chain: I
Molecule details ›
Chain: I
Length: 20 amino acids
Theoretical weight: 2.23 KDa
Source organism: Mus musculus
Expression system: Not provided

Ligands and Environments

6 bound ligands:
Ligand PO4 1 x PO4
Ligand MG 2 x MG
Ligand ADP 1 x ADP
Ligand ATP 1 x ATP
Ligand MRD 1 x MRD
Ligand GOL 1 x GOL
2 modified residues:
Ligand TPO 1 x TPO
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P212121
Unit cell:
a: 57.76Å b: 79.513Å c: 97.739Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 0.132 0.162
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

7 review citations

MAP kinases and the control of nuclear events.
Turjanski et al. (2007)
6 more

17 mentions without citation

Metal Fluorides: Tools for Structural and Computational Analysis of Phosphoryl Transfer Enzymes.
Jin et al. (2017)
16 more