› 4rkk

X-ray diffraction
2.4Å resolution

Function and Biology Details

Reactions catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131885 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Laforin Chains: A, C
Molecule details ›
Chains: A, C
Length: 332 amino acids
Theoretical weight: 37.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O95278 (Residues: 1-329; Coverage: 99%)
Gene name: EPM2A
Sequence domains:
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
2 bound ligands:
Ligand PO4 2 x PO4
Ligand GLC 2 x GLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID, null
Spacegroup: P43212
Unit cell:
a: 78.706Å b: 78.706Å c: 321.124Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.166 0.211
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Lafora disease - from pathogenesis to treatment strategies.
Nitschke et al. (2018)
7 more

13 mentions without citation

Brain Glycogen Structure and Its Associated Proteins: Past, Present and Future.
Brewer et al. (2019)
12 more