Aspergillus aculeatus galactanase

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).

Ligands and binding sites

• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
• GAL · beta-D-galactopyranose · sugar · 4 copies · chains A, B
• BMA · beta-D-mannopyranose · sugar · 2 copies · chains B
• CA · Calcium ion · metal · 7 copies · chains A, B
• EDO · 1,2-ethanediol · additive · 13 copies · chains A, B
• PEG · Di(hydroxyethyl)ether · additive · 4 copies · chains A, B
• ACT · Acetate ion · additive · 3 copies · chains A, B
• PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B
• PG6 · 1-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethane · additive · chains A
• PGE · Triethylene glycol · additive · chains B

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

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 185 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

• 6Q3R · Aspergillus aculeatus galactanase · the same entry in another collection · chain A against A, TM-score 1.00
• P48842 · AlphaFold monomer V2.0 prediction for arabinogalactan endo- beta-1,4-galactanase (P48842) · a predicted model of the same protein · chain B 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 P48842
• Elsewhere: RCSB PDB 6Q3R · PDBe 6Q3R · UniProt P48842