PDBe 4woh

X-ray diffraction
1.34Å resolution

Structure of of human dual-specificity phosphatase 22 (E24A/K28A/K30A/C88S) complexed with 4-nitrophenolphosphate

Released:
Source organism: Homo sapiens
Primary publication:
Structural analysis of human dual-specificity phosphatase 22 complexed with a phosphotyrosine-like substrate.
Acta Crystallogr F Struct Biol Commun 71 199-205 (2015)
PMID: 25664796

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 22 Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 18.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NRW4 (Residues: 1-163; Coverage: 89%)
Gene names: DUSP22, JSP1, LMWDSP2, MKPX
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 89.816Å b: 49.632Å c: 39.899Å
α: 90° β: 94.88° γ: 90°
R-values:
R R work R free
0.142 0.14 0.165
Expression system: Escherichia coli