› 5y15

X-ray diffraction
2.1Å resolution

Crystal structure of human DUSP28

Released:
DOI: 10.2210/pdb5y15/pdb
PDB entry 5y15 coloured by chain, front view.
PDB entry 5y15 coloured by chain, side view.
PDB entry 5y15 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical analysis of atypically low dephosphorylating activity of human dual-specificity phosphatase 28.
Ku B, Hong W, Keum CW, Kim M, Ryu H, Jeon D, Shin HC, Kim JH, Kim SJ, Ryu SE
PLoS One 12 e0187701 (2017)
PMID: 29121083

Function and Biology Details

Reactions catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175532 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity phosphatase 28 Chains: A, B
Molecule details ›
Chains: A, B
Length: 197 amino acids
Theoretical weight: 20.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4G0W2 (Residues: 1-176; Coverage: 100%)
Gene name: DUSP28
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P3121
Unit cell:
a: 78.952Å b: 78.952Å c: 90.258Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.219 0.269
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Structural and biochemical characterization of Siw14: A protein-tyrosine phosphatase fold that metabolizes inositol pyrophosphates.
Wang et al. (2018)
1 more

2 mentions without citation

Structural and biochemical analysis of atypically low dephosphorylating activity of human dual-specificity phosphatase 28.
Ku et al. (2017)
1 more