X-ray diffraction
2.15Å resolution

Structure of the PTP-like myo-inositol phosphatase from Selenomonas ruminantium in complex with myo-inositol-(1,4,5)-trikisphosphate


Function and Biology Details

Reaction catalysed:
Myo-inositol hexakisphosphate + H(2)O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Tyrosine specific protein phosphatases domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 342 amino acids
Theoretical weight: 39.13 KDa
Source organism: Selenomonas ruminantium
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q7WUJ1 (Residues: 28-346; Coverage: 100%)
Gene name: phyA
Sequence domains: Inositol hexakisphosphate
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 45.98Å b: 137.67Å c: 80.01Å
α: 90° β: 102.42° γ: 90°
R R work R free
0.198 0.197 0.219
Expression system: Escherichia coli BL21(DE3)