3icf

X-ray diffraction
2.3Å resolution

Structure of Protein serine/threonine phosphatase from Saccharomyces cerevisiae with similarity to human phosphatase PP5

Released:
Source organism: Saccharomyces cerevisiae
Entry authors: Singer AU, Xu X, Chang C, Cui H, Kagan O, Edwards AM, Joachimiak A, Yakunin AF, Savchenko A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-156706 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase T Chains: A, B
Molecule details ›
Chains: A, B
Length: 335 amino acids
Theoretical weight: 38.38 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P53043 (Residues: 179-513; Coverage: 65%)
Gene names: G6347, PPT1, YGR123C
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P32
Unit cell:
a: 47.194Å b: 47.194Å c: 237.096Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.19 0.24
Expression system: Escherichia coli