› 3h68

X-ray diffraction
1.5Å resolution

Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c)with two Zn2+ atoms originally soaked with cantharidin (which is present in the structure in the hydrolyzed form)

Released:
DOI: 10.2210/pdb3h68/pdb
PDB entry 3h68 coloured by chain, front view.
PDB entry 3h68 coloured by chain, side view.
PDB entry 3h68 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of serine/threonine phosphatase inhibition by the archetypal small molecules cantharidin and norcantharidin.
Bertini I, Calderone V, Fragai M, Luchinat C, Talluri E
J Med Chem 52 4838-43 (2009)
PMID: 19601647

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156702 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • Canonical: P53041 (Residues: 176-490; Coverage: 63%)
Gene names: PPP5, PPP5C
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand NHC 2 x NHC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 154.175Å b: 41.721Å c: 105.172Å
α: 90° β: 97.24° γ: 90°
R-values:
R R work R free
0.188 0.184 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Terpenoids: natural products for cancer therapy.
Huang et al. (2012)
5 more

1 mention without citation

Viewing serine/threonine protein phosphatases through the eyes of drug designers.
Zhang et al. (2013)