› 4ut2

X-ray diffraction
1.96Å resolution

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153234 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase PP1-gamma catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 323 amino acids
Theoretical weight: 37.08 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: P36873 (Residues: 1-323; Coverage: 100%)
Gene name: PPP1CC
Sequence domains:
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

2 bound ligands:
Ligand MN 4 x MN
Ligand PO4 2 x PO4
1 modified residue:
Ligand CSO 6 x CSO

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21
Unit cell:
a: 38.55Å b: 90.24Å c: 91.13Å
α: 90° β: 90.05° γ: 90°
R-values:
R R work R free
0.168 0.167 0.201
Expression system: Escherichia coli DH5[alpha]

Quick links

Citations

26 review citations

Reactive oxygen species (ROS) as pleiotropic physiological signalling agents.
Sies et al. (2020)
25 more

3 mentions without citation

Advances in indoleamine 2,3-dioxygenase 1 medicinal chemistry.
Coletti et al. (2017)
2 more