› 1fsi

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF CYCLIC NUCLEOTIDE PHOSPHODIESTERASE OF APPR>P FROM ARABIDOPSIS THALIANA

Released:
DOI: 10.2210/pdb1fsi/pdb
PDB entry 1fsi coloured by chain, front view.
PDB entry 1fsi coloured by chain, side view.
PDB entry 1fsi coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structure and mechanism of activity of the cyclic phosphodiesterase of Appr>p, a product of the tRNA splicing reaction.
Hofmann A, Zdanov A, Genschik P, Ruvinov S, Filipowicz W, Wlodawer A
EMBO J 19 6207-17 (2000)
PMID: 11080166

Function and Biology Details

Reaction catalysed: 
Nucleoside 2',3'-cyclic phosphate + H(2)O = nucleoside 2'-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-126433 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyclic phosphodiesterase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 189 amino acids
Theoretical weight: 21.51 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O04147 (Residues: 1-181; Coverage: 100%)
Gene names: At4g18930, F13C5.100, F13C5_100
Sequence domains: Cyclic phosphodiesterase-like protein
Structure domains: Cyclic phosphodiesterase

Ligands and Environments

1 bound ligand:
Ligand SO4 9 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P6122
Unit cell:
a: 125.916Å b: 125.916Å c: 209.897Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.196 0.265
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Nuclear ADP-Ribosylation and Its Role in Chromatin Plasticity, Cell Differentiation, and Epigenetics.
Hottiger MO. (2015)
4 more

9 mentions without citation

Urokinase-type plasminogen activator receptor (uPAR) as a therapeutic target in cancer.
Zhai et al. (2022)
8 more