2g59

X-ray diffraction
2.19Å resolution

Crystal Structure of the Catalytic Domain of Protein Tyrosine Phosphatase from Homo sapiens

Released:

Function and Biology Details

Reaction catalysed:
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor-type tyrosine-protein phosphatase O Chains: A, B
Molecule details ›
Chains: A, B
Length: 297 amino acids
Theoretical weight: 34.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16827 (Residues: 914-1200; Coverage: 24%)
Gene names: GLEPP1, PTPRO, PTPU2
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P21
Unit cell:
a: 73.869Å b: 59.723Å c: 76.995Å
α: 90° β: 102.31° γ: 90°
R-values:
R R work R free
0.199 0.199 0.237
Expression system: Escherichia coli