› 5y16

X-ray diffraction
2.4Å resolution

Crystal structure of human DUSP28(Y102H)

Released:
DOI: 10.2210/pdb5y16/pdb
PDB entry 5y16 coloured by chain, front view.
PDB entry 5y16 coloured by chain, side view.
PDB entry 5y16 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: 20.58 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

2 bound ligands:
Ligand PO4 2 x PO4
Ligand CL 3 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P3121
Unit cell:
a: 79.341Å b: 79.341Å c: 90.549Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.187 0.24
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

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

1 mention without citation

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