4r30

X-ray diffraction
2.3Å resolution

Structure of human laforin dual specificity phosphatase domain

Released:
Source organism: Homo sapiens
Primary publication:
Dimeric quaternary structure of human laforin.
J Biol Chem 290 4552-4559 (2015)
PMID: 25538239

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131884 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Laforin Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 184 amino acids
Theoretical weight: 21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O95278 (Residues: 148-331; Coverage: 56%)
Gene name: EPM2A
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: I41
Unit cell:
a: 123.974Å b: 123.974Å c: 160.771Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.188 0.219
Expression system: Escherichia coli BL21