PDBe 4b04

X-ray diffraction
2.2Å resolution

Crystal structure of the Catalytic Domain of Human DUSP26 (C152S)

Released:
Source organism: Homo sapiens

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 26 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 160 amino acids
Theoretical weight: 18.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 82.6Å b: 82.78Å c: 91.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.2 0.266
Expression system: Escherichia coli BL21(DE3)