PDBe 3f5g

X-ray diffraction
1.85Å resolution

Crystal structure of death associated protein kinase in complex with ADP and Mg2+

Released:
Source organism: Homo sapiens
Primary publication:
Structural insight into nucleotide recognition by human death-associated protein kinase.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. 65 241-8 (2009)
PMID: 19237746

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:
Death-associated protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53355 (Residues: 2-285; Coverage: 20%)
Gene names: DAPK, DAPK1
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: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 46.807Å b: 62.545Å c: 88.396Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.244
Expression system: Escherichia coli