Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation H230S, crystallized with 2',3-(rp)- cyclic-amps

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 31% strand (DSSP).

Ligands and binding sites

• QQY · [(3aR,4R,6R,6aR)-4-(6-aminopurin-9-yl)-2-oxidanylidene-2-sulfanyl-3a,4,6,6a-tetrahydrofuro[3,4-d][1,3,2]dioxaphosphol-6-yl]methanol · ligand · chains A
• CL · Chloride ion · ion · chains A
• ACT · Acetate ion · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Compared structures

• 2YPH · Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation… · the same entry in another collection · chain A against A, TM-score 1.00
• P16330 · AlphaFold monomer V2.0 prediction for 2',3'-cyclic-nucleotide 3'-phosphodiesterase… · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P16330
• Elsewhere: RCSB PDB 2YPH · PDBe 2YPH · UniProt P16330