› 3h66

X-ray diffraction
2.59Å resolution

Catalytic domain of human Serine/Threonine Phosphatase 5 (PP5c) with two Zn2+ atoms

Released:
DOI: 10.2210/pdb3h66/pdb
PDB entry 3h66 coloured by chain, front view.
PDB entry 3h66 coloured by chain, side view.
PDB entry 3h66 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, B
Molecule details ›
Chains: A, B
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

1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION ENHANCE ULTRA
Spacegroup: C2
Unit cell:
a: 154.251Å b: 41.684Å c: 106.092Å
α: 90° β: 96.46° γ: 90°
R-values:
R R work R free
0.208 0.199 0.291
Expression system: Escherichia coli BL21(DE3)

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Citations

7 review citations

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