› 2g62

X-ray diffraction
1.6Å resolution

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172238 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase 2A activator Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 37.33 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q15257 (Residues: 22-358; Coverage: 84%)
Gene names: PPP2R4, PTPA
Sequence domains: Phosphotyrosyl phosphate activator (PTPA) protein
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 48.19Å b: 76.42Å c: 87.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.183
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Assembly and structure of protein phosphatase 2A.
Shi Y. (2009)
1 more

5 mentions without citation

Determination and validation of principal gene products.
Tress et al. (2008)
4 more