› 4g9j

X-ray diffraction
3.1Å resolution

Protein Ser/Thr phosphatase-1 in complex with cell-permeable peptide

Released:
DOI: 10.2210/pdb4g9j/pdb
PDB entry 4g9j coloured by chain, front view.
PDB entry 4g9j coloured by chain, side view.
PDB entry 4g9j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Development of a peptide that selectively activates protein phosphatase-1 in living cells.
Chatterjee J, Beullens M, Sukackaite R, Qian J, Lesage B, Hart DJ, Bollen M, Köhn M
Angew Chem Int Ed Engl 51 10054-9 (2012)
PMID: 22962028

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158549 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 331 amino acids
Theoretical weight: 37.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P62136 (Residues: 1-330; Coverage: 100%)
Gene names: PPP1A, PPP1CA
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2
synthetic peptide Chains: C, D
Molecule details ›
Chains: C, D
Length: 23 amino acids
Theoretical weight: 2.81 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P42212
Unit cell:
a: 138.007Å b: 138.007Å c: 113.675Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.224 0.276
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

7 review citations

Targeting the untargetable: recent advances in the selective chemical modulation of protein phosphatase-1 activity.
Chatterjee et al. (2013)
6 more

7 mentions without citation

Intrinsic Disorder and Posttranslational Modifications: The Darker Side of the Biological Dark Matter.
Darling et al. (2018)
6 more