PDBe 2esb

X-ray diffraction
2Å resolution

Crystal structure of human DUSP18

Source organism: Homo sapiens
Primary publication:
Structure of human DSP18, a member of the dual-specificity protein tyrosine phosphatase family.
Acta Crystallogr. D Biol. Crystallogr. 62 582-8 (2006)
PMID: 16699184

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Dual specificity protein phosphatase 18 Chain: A
Molecule details ›
Chain: A
Length: 188 amino acids
Theoretical weight: 21.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q8NEJ0 (Residues: 1-188; Coverage: 100%)
Gene names: DUSP18, LMWDSP20
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: C2221
Unit cell:
a: 35.74Å b: 96.083Å c: 116.654Å
α: 90° β: 90° γ: 90°
R R work R free
0.161 0.159 0.189
Expression system: Escherichia coli