2e0t

X-ray diffraction
1.67Å resolution

Crystal structure of catalytic domain of dual specificity phosphatase 26, MS0830 from Homo sapiens

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:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-189750 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 26 Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 17.05 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9BV47 (Residues: 61-211; Coverage: 72%)
Gene names: DUSP24, DUSP26, LDP4, MKP8, NATA1, SKRP3
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL12B2, APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 80.721Å b: 40.176Å c: 49.944Å
α: 90° β: 110.35° γ: 90°
R-values:
R R work R free
0.172 0.172 0.212
Expression system: Not provided