› 6spy

X-ray diffraction
1.6Å resolution

Crystal structure of cAMP-dependent protein kinase A (CHO PKA) in complex with 6-(morpholin-4-yl)pyridine-3-carboxamide

Released:
DOI: 10.2210/pdb6spy/pdb
PDB entry 6spy coloured by chain, front view.
PDB entry 6spy coloured by chain, side view.
PDB entry 6spy coloured by chain, top view.
Source organism: Cricetulus griseus
Primary publication:
Fragment Binding to Kinase Hinge: If Charge Distribution and Local pKa Shifts Mislead Popular Bioisosterism Concepts.
Oebbeke M, Siefker C, Wagner B, Heine A, Klebe G
OpenAccess logo Angew Chem Int Ed Engl 60 252-258 (2021)
PMID: 33021032

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150424 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
cAMP-dependent protein kinase catalytic subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 41.11 KDa
Source organism: Cricetulus griseus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P25321 (Residues: 1-351; Coverage: 100%)
Gene name: PRKACA
Sequence domains: Protein kinase domain

Ligands and Environments

3 bound ligands:
Ligand LR8 1 x LR8
Ligand DMS 1 x DMS
Ligand MPD 1 x MPD
2 modified residues:
Ligand SEP 2 x SEP
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 51.512Å b: 71.34Å c: 97.496Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.182
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 citation in other articles

Frag4Lead: growing crystallographic fragment hits by catalog using fragment-guided template docking.
Metz et al. (2021)
4 more

1 mention without citation

Fragment Binding to Kinase Hinge: If Charge Distribution and Local pKa Shifts Mislead Popular Bioisosterism Concepts.
Oebbeke et al. (2021)