PDBe 1yz4

X-ray diffraction
2.4Å resolution

Crystal structure of DUSP15

Released:

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 15 Chains: A, B
Molecule details ›
Chains: A, B
Length: 160 amino acids
Theoretical weight: 17.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9H1R2 (Residues: 1-146; Coverage: 49%)
  • Best match: Q9H1R2-4 (Residues: 1-21, 22-54)
Gene names: C20orf57, DUSP15, VHY
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: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 43.233Å b: 76.395Å c: 101.429Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.217 0.269
Expression system: Escherichia coli BL21(DE3)