› 2ixm

X-ray diffraction
1.5Å 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: 303 amino acids
Theoretical weight: 34.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15257 (Residues: 20-357; Coverage: 85%)
Gene names: PPP2R4, PTPA
Sequence domains: Phosphotyrosyl phosphate activator (PTPA) protein
Structure domains: Four Helix Bundle (Hemerythrin (Met), subunit A)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 48.243Å b: 70.41Å c: 95.534Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.202 0.221
Expression system: Escherichia coli

Quick links

Citations

11 review citations

Serine/threonine phosphatases: mechanism through structure.
Shi Y. (2009)
10 more

2 mentions without citation

Protein structure prediction guided by crosslinking restraints--A systematic evaluation of the impact of the crosslinking spacer length.
Hofmann et al. (2015)
1 more