GH51 a-L-arabinofuranosidase soaked with aziridine inhibitor

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).

Ligands and binding sites

• LXE · [(1~{S},2~{S},3~{S},4~{S})-2-(hydroxymethyl)-3,4-bis(oxidanyl)cyclopentyl]azanium · ligand · 2 copies · chains A, B
• ETE · 2-{2-[2-2-(methoxy-ethoxy)-ethoxy]-ethoxy}-ethanol · ligand · chains B
• GOL · Glycerol · additive · 9 copies · chains A, B
• PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
• PGE · Triethylene glycol · additive · chains A

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 829 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

• 6SXV · GH51 a-l-arabinofuranosidase soaked with aziridine inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
• Q9XBQ3 · AlphaFold monomer V2.0 prediction for intracellular exo… · a predicted model of the same protein · chain A against A, TM-score 1.00

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 Q9XBQ3
• Elsewhere: RCSB PDB 6SXV · PDBe 6SXV · UniProt Q9XBQ3