› 4ylj

X-ray diffraction
2.58Å resolution

Crystal structure of DYRK1A in complex with 10-Iodo-substituted 11H-indolo[3,2-c]quinoline-6-carboxylic acid inhibitor 5j

Released:
DOI: 10.2210/pdb4ylj/pdb
PDB entry 4ylj coloured by chain, front view.
PDB entry 4ylj coloured by chain, side view.
PDB entry 4ylj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
10-iodo-11H-indolo[3,2-c]quinoline-6-carboxylic acids are selective inhibitors of DYRK1A.
Falke H, Chaikuad A, Becker A, Loaëc N, Lozach O, Abu Jhaisha S, Becker W, Jones PG, Preu L, Baumann K, Knapp S, Meijer L, Kunick C
J Med Chem 58 3131-43 (2015)
PMID: 25730262

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: 361 amino acids
Theoretical weight: 42.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13627 (Residues: 127-485; Coverage: 47%)
Gene names: DYRK, DYRK1A, MNB, MNBH
Sequence domains: Protein kinase domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand PG4 7 x PG4
Ligand SO4 10 x SO4
Ligand 4E1 4 x 4E1
1 modified residue:
Ligand PTR 4 x PTR

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: C2
Unit cell:
a: 265.472Å b: 65.528Å c: 139.365Å
α: 90° β: 114.6° γ: 90°
R-values:
R R work R free
0.193 0.192 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Pharmacology of Modulators of Alternative Splicing.
Bates et al. (2017)
5 more

7 mentions without citation

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