2g6z

X-ray diffraction
2.7Å resolution

Crystal structure of human DUSP5

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 trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 5 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 211 amino acids
Theoretical weight: 23.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16690 (Residues: 178-384; Coverage: 54%)
Gene names: DUSP5, VH3
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: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P4322
Unit cell:
a: 92.712Å b: 92.712Å c: 165.213Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.244 0.291
Expression system: Escherichia coli