PDBe 1zws

X-ray diffraction
2.9Å resolution

Crystal structure of the catalytic domain of human DRP-1 kinase

Released:
Source organism: Homo sapiens
Entry authors: Kursula P, Schunck H, Wilmanns M

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 dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Death-associated protein kinase 2 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 288 amino acids
Theoretical weight: 33.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UIK4 (Residues: 11-297; Coverage: 78%)
Gene name: DAPK2
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: MAX II BEAMLINE I711
Spacegroup: P21
Unit cell:
a: 52.62Å b: 211.83Å c: 128.42Å
α: 90° β: 101.82° γ: 90°
R-values:
R R work R free
0.22 0.22 0.258
Expression system: Escherichia coli