PDBe 3a2c

X-ray diffraction
2.9Å resolution

Crystal structure of a pyrazolopyrimidine inhibitor complex bound to MAPKAP Kinase-2 (MK2)

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:
homo 12-mer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MAP kinase-activated protein kinase 2 Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 324 amino acids
Theoretical weight: 37.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49137 (Residues: 41-364; Coverage: 81%)
Gene name: MAPKAPK2
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32B2
Spacegroup: P212121
Unit cell:
a: 139.157Å b: 180.956Å c: 216.096Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.288 0.288 0.335
Expression system: Escherichia coli BL21(DE3)