› 5aux

X-ray diffraction
1.5Å resolution

Crystal structure of DAPK1 in complex with kaempferol.

Released:
DOI: 10.2210/pdb5aux/pdb
PDB entry 5aux coloured by chain, front view.
PDB entry 5aux coloured by chain, side view.
PDB entry 5aux coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural Insight into the Interactions between Death-Associated Protein Kinase 1 and Natural Flavonoids.
Yokoyama T, Kosaka Y, Mizuguchi M
J Med Chem 58 7400-8 (2015)
PMID: 26322379

Function and Biology Details

Reaction catalysed: 
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156788 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Death-associated protein kinase 1 Chain: A
Molecule details ›
Chain: A
Length: 293 amino acids
Theoretical weight: 33.8 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

2 bound ligands:
Ligand KMP 1 x KMP
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 46.823Å b: 62.193Å c: 88.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.208
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Death-associated protein kinase (DAPK) family modulators: Current and future therapeutic outcomes.
Farag et al. (2019)
10 more

4 mentions without citation

Involvement of three putative glucosyltransferases from the UGT72 family in flavonol glucoside/rhamnoside biosynthesis in Lotus japonicus seeds.
Yin et al. (2017)
3 more