› 5y86

X-ray diffraction
1.9Å resolution

Crystal structure of kinase

Released:
DOI: 10.2210/pdb5y86/pdb
PDB entry 5y86 coloured by chain, front view.
PDB entry 5y86 coloured by chain, side view.
PDB entry 5y86 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal Structure of Human Dual-Specificity Tyrosine-Regulated Kinase 3 Reveals New Structural Features and Insights into its Auto-phosphorylation.
Kim K, Cha JS, Cho YS, Kim H, Chang N, Kim HJ, Cho HS
J Mol Biol 430 1521-1530 (2018)
PMID: 29634919

Function and Biology Details

Reaction catalysed: 
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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129108 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity tyrosine-phosphorylation-regulated kinase 3 Chain: A
Molecule details ›
Chain: A
Length: 588 amino acids
Theoretical weight: 66.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43781 (Residues: 1-588; Coverage: 100%)
Gene name: DYRK3
Sequence domains: Protein kinase domain

Ligands and Environments

4 bound ligands:
Ligand HRM 1 x HRM
Ligand PO4 2 x PO4
Ligand EDO 8 x EDO
Ligand GOL 1 x GOL
3 modified residues:
Ligand SEP 2 x SEP
Ligand PTR 1 x PTR
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Unit cell:
a: 43Å b: 76.52Å c: 148.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.167 0.196
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Updating dual-specificity tyrosine-phosphorylation-regulated kinase 2 (DYRK2): molecular basis, functions and role in diseases.
Correa-Sáez et al. (2020)
3 other articles

5 mentions without citation

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