› 4ij9

X-ray diffraction
2.55Å resolution

Bovine PKA C-alpha in complex with 2-[[5-(4-pyridyl)-1H-1,2,4-triazol-3-yl]sulfanyl]-1-(2-thiophenyl)ethanone

Released:
DOI: 10.2210/pdb4ij9/pdb
PDB entry 4ij9 coloured by chain, front view.
PDB entry 4ij9 coloured by chain, side view.
PDB entry 4ij9 coloured by chain, top view.
Source organisms:
Primary publication:
Accounting for conformational variability in protein-ligand docking with NMR-guided rescoring.
Skjærven L, Codutti L, Angelini A, Grimaldi M, Latek D, Monecke P, Dreyer MK, Carlomagno T
J Am Chem Soc 135 5819-27 (2013)
PMID: 23565800

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132590 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
cAMP-dependent protein kinase catalytic subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 350 amino acids
Theoretical weight: 40.71 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00517 (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: 20 amino acids
Theoretical weight: 2.23 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P61925 (Residues: 6-25; Coverage: 26%)
Gene names: PKIA, PRKACN1

Ligands and Environments

1 bound ligand:
Ligand PTV 1 x PTV
2 modified residues:
Ligand TPO 1 x TPO
Ligand SEP 1 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 72.68Å b: 75.61Å c: 79.05Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.17 0.248
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Improvements, trends, and new ideas in molecular docking: 2012-2013 in review.
Yuriev et al. (2015)
2 more

1 mention without citation

An approach to creating a more realistic working model from a protein data bank entry.
Brandon et al. (2015)