2y96

X-ray diffraction
2.38Å resolution

Structure of human dual-specificity phosphatase 27

Released:
Source organism: Homo sapiens
Primary publication:
Structure of human dual-specificity phosphatase 27 at 2.38 Å resolution.
Acta Crystallogr D Biol Crystallogr 67 471-9 (2011)
PMID: 21543850

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-179346 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity phosphatase 29 Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 25.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q68J44 (Residues: 2-220; Coverage: 100%)
Gene names: DUPD1, DUSP27, DUSP29
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: APS BEAMLINE 22-BM
Spacegroup: P6422
Unit cell:
a: 126.012Å b: 126.012Å c: 125.758Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.201 0.225
Expression system: Escherichia coli BL21(DE3)