2hxp

X-ray diffraction
1.83Å resolution

Crystal Structure of the human phosphatase (DUSP9)

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)
PDBe Complex ID:
PDB-CPX-573091 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 9 Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99956 (Residues: 201-345; Coverage: 38%)
Gene names: DUSP9, MKP4
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: NSLS BEAMLINE X12C
Spacegroup: P32
Unit cell:
a: 50.527Å b: 50.527Å c: 59.851Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.216 0.246
Expression system: Escherichia coli