› 1o1z

X-ray diffraction
1.6Å resolution

Function and Biology Details

Reaction catalysed: 
A glycerophosphodiester + H(2)O = an alcohol + sn-glycerol 3-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194840 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GP-PDE domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 234 amino acids
Theoretical weight: 27.17 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1V6 (Residues: 2-222; Coverage: 100%)
Gene name: TM_1621
Sequence domains: Glycerophosphoryl diester phosphodiesterase family
Structure domains: Phosphatidylinositol (PI) phosphodiesterase

Ligands and Environments

1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21212
Unit cell:
a: 132.41Å b: 41.79Å c: 51.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 0.139 0.18
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
2 more

8 mentions without citation

Computational and biochemical analysis of the Xanthomonas effector AvrBs2 and its role in the modulation of Xanthomonas type three effector delivery.
Zhao et al. (2011)
7 more