2vx3

X-ray diffraction
2.4Å resolution

Crystal structure of the human dual specificity tyrosine- phosphorylation-regulated kinase 1A

Released:

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 382 amino acids
Theoretical weight: 44.55 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

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 264.203Å b: 65.105Å c: 140.282Å
α: 90° β: 115.44° γ: 90°
R-values:
R R work R free
0.186 0.185 0.23
Expression system: Escherichia coli BL21(DE3)