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Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with mutation V321A, crystallized with 2'-amps

Analyse Catalytic domain of mouse 2',3'-cyclic nucleotide 3'- phosphodiesterase, with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ZBZ
Type
protein
Length
208 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
2', 3'-cyclic-nucleotide 3'-phosphodiesterase
EC
3.1.4.37
UniProt
P16330
Ligands
OVE
Pockets
2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A2', 3'-cyclic-nucleotide 3'-phosphodiesterase (EC 3.1.4.37)protein20831% helix, 32% strandP16330

Ligands and binding sites

  • OVE · 2'-O-(sulfidophosphinato)adenosine · ligand · chains A
  • ACY · Acetic acid · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13600.590.7638OVE
2600.480.8516empty

Compared structures

  • 3ZBZ · 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

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