PDBe 2z72

X-ray diffraction
1.1Å resolution

New Structure Of Cold-Active Protein Tyrosine Phosphatase At 1.1 Angstrom

Released:

Function and Biology Details

Reaction catalysed:
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. 
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-tyrosine-phosphatase Chain: A
Molecule details ›
Chain: A
Length: 342 amino acids
Theoretical weight: 38.85 KDa
Source organism: Shewanella sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9S427 (Residues: 22-361; Coverage: 100%)
Gene name: PPI
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL38B1
Spacegroup: P212121
Unit cell:
a: 55.565Å b: 77.306Å c: 81.029Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.116 not available 0.161
Expression system: Escherichia coli