PDBe 3fyj

X-ray diffraction
3.8Å resolution

Crystal structure of an optimzied benzothiophene inhibitor bound to MAPKAP Kinase-2 (MK-2)

Released:

Function and Biology Details

Reaction catalysed:
ATP + a protein = ADP + a phosphoprotein. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo trimer
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MAP kinase-activated protein kinase 2 Chain: X
Molecule details ›
Chain: X
Length: 327 amino acids
Theoretical weight: 37.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P49137 (Residues: 45-371; Coverage: 82%)
Gene name: MAPKAPK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: F4132
Unit cell:
a: 255.551Å b: 255.551Å c: 255.551Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.331 0.328 0.388
Expression system: Escherichia coli