› 3e7b

X-ray diffraction
1.7Å resolution

Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin inhibitor Tautomycin

Released:
DOI: 10.2210/pdb3e7b/pdb
PDB entry 3e7b coloured by chain, front view.
PDB entry 3e7b coloured by chain, side view.
PDB entry 3e7b coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors.
Kelker MS, Page R, Peti W
J Mol Biol 385 11-21 (2009)
PMID: 18992256

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-158547 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 299 amino acids
Theoretical weight: 34.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62136 (Residues: 7-300; Coverage: 89%)
Gene names: PPP1A, PPP1CA
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

6 bound ligands:
Ligand MN 4 x MN
Ligand E7B 2 x E7B
Ligand CL 1 x CL
Ligand GOL 1 x GOL
Ligand NA 1 x NA
Ligand AZI 6 x AZI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P212121
Unit cell:
a: 65.76Å b: 78.519Å c: 130.764Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.175
Expression system: Escherichia coli

Quick links

Citations

16 review citations

The extended PP1 toolkit: designed to create specificity.
Bollen et al. (2010)
15 more

13 mentions without citation

Structural basis for protein phosphatase 1 regulation and specificity.
Peti et al. (2013)
12 more