PDBe 2p3g

X-ray diffraction
3.8Å resolution

Crystal structure of a pyrrolopyridine inhibitor bound to MAPKAP Kinase-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

Assembly composition:
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 BL21(DE3)
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: 253.941Å b: 253.941Å c: 253.941Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.303 0.3 0.374
Expression system: Escherichia coli BL21(DE3)