4wfr

X-ray diffraction
2Å resolution

Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation T232A, complexed with 2'-AMP

Released:

Function and Biology Details

Reaction catalysed:
Nucleoside 2',3'-cyclic phosphate + H(2)O = nucleoside 2'-phosphate
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2',3'-cyclic-nucleotide 3'-phosphodiesterase Chain: A
Molecule details ›
Chain: A
Length: 221 amino acids
Theoretical weight: 24.26 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P16330 (Residues: 179-398; Coverage: 52%)
Gene names: Cnp, Cnp1
Structure domains: 2',3'-cyclic nucleotide 3'-phosphodiesterase superfamily

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P21
Unit cell:
a: 41.77Å b: 47.094Å c: 53.951Å
α: 90° β: 94.36° γ: 90°
R-values:
R R work R free
0.219 0.216 0.266
Expression system: Escherichia coli BL21(DE3)