4ki9

X-ray diffraction
2Å resolution

Crystal structure of the catalytic domain of human DUSP12 at 2.0 A resolution

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
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-193996 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dual specificity protein phosphatase 12 Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 18.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UNI6 (Residues: 27-189; Coverage: 48%)
Gene name: DUSP12
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: PAL/PLS BEAMLINE 5C (4A), PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P41212
Unit cell:
a: 50.55Å b: 50.55Å c: 128.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.169 0.214
Expression system: Escherichia coli