› 1a17

X-ray diffraction
2.45Å resolution

TETRATRICOPEPTIDE REPEATS OF PROTEIN PHOSPHATASE 5

Released:
DOI: 10.2210/pdb1a17/pdb
PDB entry 1a17 coloured by chain, front view.
PDB entry 1a17 coloured by chain, side view.
PDB entry 1a17 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions.
Das AK, Cohen PW, Barford D
EMBO J 17 1192-9 (1998)
PMID: 9482716

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156703 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase 5 Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 19.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P53041 (Residues: 16-181; Coverage: 33%)
Gene names: PPP5, PPP5C
Sequence domains:
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: I422
Unit cell:
a: 90.06Å b: 90.06Å c: 104.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.201 0.298
Expression system: Escherichia coli

Quick links

Citations

97 review citations

14-3-3 proteins: structure, function, and regulation.
Fu et al. (2000)
96 more

31 mentions without citation

Ligand binding by repeat proteins: natural and designed.
Grove et al. (2008)
30 more