3h62

X-ray diffraction
1.4Å resolution

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

Released:

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
Macromolecule:
Serine/threonine-protein phosphatase 5 Chains: B, C
Molecule details ›
Chains: B, C
Length: 315 amino acids
Theoretical weight: 35.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • 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: 154.535Å b: 41.518Å c: 97.502Å
α: 90° β: 103.44° γ: 90°
R-values:
R R work R free
0.179 0.176 0.204
Expression system: Escherichia coli BL21(DE3)