› 4ja9

X-ray diffraction
2.3Å resolution

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:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156705 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase 5 Chain: A
Molecule details ›
Chain: A
Length: 488 amino acids
Theoretical weight: 55.8 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P53042 (Residues: 16-499; Coverage: 97%)
Gene name: Ppp5c
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P41212
Unit cell:
a: 50.09Å b: 50.09Å c: 379.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.238 0.272
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Structure, Function, and Regulation of the Hsp90 Machinery.
Biebl et al. (2019)
3 more

4 mentions without citation

The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90.
Haslbeck et al. (2015)
3 more