4y2e

X-ray diffraction
1.67Å resolution

Crystal structure of the catalytic domain of human dual-specificity phosphatase 7 (C232S)

Released:
Source organism: Homo sapiens
Primary publication:
Structure of human dual-specificity phosphatase 7, a potential cancer drug target.
Acta Crystallogr F Struct Biol Commun 71 650-6 (2015)
PMID: 26057789

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)
PDBe Complex ID:
PDB-CPX-172589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 7 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 149 amino acids
Theoretical weight: 16.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16829 (Residues: 240-388; Coverage: 36%)
Gene names: DUSP7, PYST2
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: P21
Unit cell:
a: 64.549Å b: 64.458Å c: 74.333Å
α: 90° β: 91.68° γ: 90°
R-values:
R R work R free
0.157 0.155 0.189
Expression system: Escherichia coli