› 3f81

X-ray diffraction
1.9Å resolution

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156342 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 183 amino acids
Theoretical weight: 20.28 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P51452 (Residues: 3-185; Coverage: 99%)
Gene names: DUSP3, VHR
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P21
Unit cell:
a: 50.406Å b: 59.186Å c: 60.656Å
α: 90° β: 98.36° γ: 90°
R-values:
R R work R free
0.18 0.178 0.219
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Small molecule tools for functional interrogation of protein tyrosine phosphatases.
He et al. (2013)
8 more

8 mentions without citation

Critical Roles of Dual-Specificity Phosphatases in Neuronal Proteostasis and Neurological Diseases.
Bhore et al. (2017)
7 more