PDBe 2wgp

X-ray diffraction
1.88Å resolution

Crystal structure of human dual specificity phosphatase 14

Released:
Source organism: Homo sapiens
Primary publication:
Overproduction, purification and structure determination of human dual-specificity phosphatase 14.
Acta Crystallogr. D Biol. Crystallogr. 65 1013-20 (2009)
PMID: 19770498

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. 
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo octamer
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 14 Chains: A, B
Molecule details ›
Chains: A, B
Length: 190 amino acids
Theoretical weight: 21.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95147 (Residues: 2-191; Coverage: 96%)
Gene names: DUSP14, MKP6
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: I4
Unit cell:
a: 85.011Å b: 85.011Å c: 115.112Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.175 0.221
Expression system: Escherichia coli