› 6a1f

X-ray diffraction
1.5Å resolution

Crystal structure of human DYRK1A in complex with compound 14

Released:
DOI: 10.2210/pdb6a1f/pdb
PDB entry 6a1f coloured by chain, front view.
PDB entry 6a1f coloured by chain, side view.
PDB entry 6a1f coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of DS42450411 as a potent orally active hepcidin production inhibitor: Design and optimization of novel 4-aminopyrimidine derivatives.
Fukuda T, Ishiyama T, Katagiri T, Ueda K, Muramatsu S, Hashimoto M, Aki A, Baba D, Watanabe K, Tanaka N
Bioorg Med Chem Lett 28 3333-3337 (2018)
PMID: 30217414

Function and Biology Details

Reactions catalysed: 
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171789 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity tyrosine-phosphorylation-regulated kinase 1A Chain: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 41.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13627 (Residues: 127-483; Coverage: 47%)
Gene names: DYRK, DYRK1A, MNB, MNBH
Sequence domains: Protein kinase domain

Ligands and Environments

3 bound ligands:
Ligand SO4 6 x SO4
Ligand 9OF 1 x 9OF
Ligand PGE 1 x PGE
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: C2
Unit cell:
a: 99.341Å b: 69.806Å c: 67.332Å
α: 90° β: 117.65° γ: 90°
R-values:
R R work R free
0.178 0.177 0.195
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 mention without citation

Dual-Specificity, Tyrosine Phosphorylation-Regulated Kinases (DYRKs) and cdc2-Like Kinases (CLKs) in Human Disease, an Overview.
Lindberg et al. (2021)