X-ray diffraction
1.9Å resolution

Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Mn2+ atoms complexed with endothall


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Serine/threonine-protein phosphatase 5 Chains: A, D
Molecule details ›
Chains: A, D
Length: 315 amino acids
Theoretical weight: 35.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P53041 (Residues: 176-490; Coverage: 63%)
Gene names: PPP5, PPP5C
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2
Unit cell:
a: 154.553Å b: 41.463Å c: 95.614Å
α: 90° β: 96.78° γ: 90°
R R work R free
0.195 0.19 0.237
Expression system: Escherichia coli BL21(DE3)