› 4i15

X-ray diffraction
1.65Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphodiesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 343 amino acids
Theoretical weight: 38.72 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8WQX9 (Residues: 576-918; Coverage: 37%)
Gene name: PDEB1
Sequence domains: 3'5'-cyclic nucleotide phosphodiesterase
Structure domains: 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 115.007Å b: 115.337Å c: 68.506Å
α: 90° β: 108.13° γ: 90°
R-values:
R R work R free
0.204 0.204 0.223
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Druggable Targets in Cyclic Nucleotide Signaling Pathways in Apicomplexan Parasites and Kinetoplastids against Disabling Protozoan Diseases in Humans.
Kaiser A. (2019)
6 more

8 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
7 more