2y4p

X-ray diffraction
2.65Å resolution

Dimeric structure of DAPK-1 catalytic domain

Released:
Source organism: Homo sapiens
Entry authors: de Diego I, Lehmann F, 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)
PDBe Complex ID:
PDB-CPX-156790 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Death-associated protein kinase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 285 amino acids
Theoretical weight: 32.73 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 83.94Å b: 73.7Å c: 120.28Å
α: 90° β: 101.24° γ: 90°
R-values:
R R work R free
0.255 0.252 0.312
Expression system: Escherichia coli BL21(DE3)