PDBe 3dgk

X-ray diffraction
1.7Å resolution

Crystal structure of a glycine-rich loop mutant of the death associated protein kinase catalytic domain

Released:
Source organism: Homo sapiens
Entry authors: McNamara LK, Schavocky JP, Watterson DM, Brunzelle JS

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: 295 amino acids
Theoretical weight: 33.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53355 (Residues: 1-285; Coverage: 20%)
Gene names: DAPK, DAPK1
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 47.208Å b: 62.441Å c: 88.576Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.173 0.22
Expression system: Escherichia coli