Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal exo-beta-D-N-acetylglucosaminidase, strh

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).

Ligands and binding sites

• NGW · (2S,3aR,5R,6S,7R,7aR)-5-(hydroxymethyl)-2-methyl-2,3a,5,6,7,7a-hexahydro-1H-pyrano[3,2-d][1,3]thiazole-6,7-diol · ligand · chains A
• MG · Magnesium ion · metal · 4 copies · chains A
• EDO · 1,2-ethanediol · additive · 3 copies · chains A
• PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · 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

• 4AZ5 · Differential inhibition of the tandem GH20 catalytic modules in the pneumococcal… · the same entry in another collection · chain A against A, TM-score 1.00
• P49610 · AlphaFold monomer V2.0 prediction for beta-N-acetylhexosaminidase (P49610) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P49610
• Elsewhere: RCSB PDB 4AZ5 · PDBe 4AZ5 · UniProt P49610