› 5a4t

X-ray diffraction
2.15Å resolution

DYRK1A IN COMPLEX WITH NITRILE BENZOTHIAZOLE FRAGMENT

Released:
DOI: 10.2210/pdb5a4t/pdb
PDB entry 5a4t coloured by chain, front view.
PDB entry 5a4t coloured by chain, side view.
PDB entry 5a4t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Probing the ATP-Binding Pocket of Protein Kinase DYRK1A with Benzothiazole Fragment Molecules.
Rothweiler U, Stensen W, Brandsdal BO, Isaksson J, Leeson FA, Engh RA, Svendsen JS
J Med Chem 59 9814-9824 (2016)
PMID: 27736065

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 368 amino acids
Theoretical weight: 42.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13627 (Residues: 126-490; Coverage: 48%)
Gene names: DYRK, DYRK1A, MNB, MNBH
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand AJG 4 x AJG
1 modified residue:
Ligand PTR 4 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 87.753Å b: 87.702Å c: 229.611Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A) inhibitors: a survey of recent patent literature.
Nguyen et al. (2017)
1 more

1 mention without citation

A facile consensus ranking approach enhances virtual screening robustness and identifies a cell-active DYRK1α inhibitor.
Mavrogeni et al. (2018)