› 4z0v

X-ray diffraction
1.78Å resolution

Function and Biology Details

Reaction catalysed: 
Exonucleolytic cleavage of poly(A) to 5'-AMP
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179850 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2',5'-phosphodiesterase 12 Chain: A
Molecule details ›
Chain: A
Length: 440 amino acids
Theoretical weight: 49.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6L8Q7 (Residues: 155-609; Coverage: 72%)
Gene name: PDE12
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand GOL 6 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 56.688Å b: 62.554Å c: 65.393Å
α: 90° β: 110.4° γ: 90°
R-values:
R R work R free
0.166 0.164 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

DNA-encoded chemistry: enabling the deeper sampling of chemical space.
Goodnow et al. (2017)
12 more

2 mentions without citation

The Role of Phosphodiesterase 12 (PDE12) as a Negative Regulator of the Innate Immune Response and the Discovery of Antiviral Inhibitors.
Wood et al. (2015)
1 more