Refined structure for the complex of acarbose with glucoamylase from aspergillus awamori var. X100 to 2.4 ångströms resolution

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 7% strand (DSSP).

Ligands and binding sites

• AC1 · 4,6-dideoxy-4-{[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranose · ligand · 2 copies · chains A
• MAN · alpha-D-mannopyranose · sugar · 17 copies · chains A
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
• GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A
• BMA · beta-D-mannopyranose · sugar · 2 copies · 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, 2 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 12 glycan, 3 disulfide (O-glycosylation, disulfide, N-glycosylation).

Compared structures

• 1AGM · Refined structure for the complex of acarbose with glucoamylase from Aspergillus awamori… · the same entry in another collection · chain A against A, TM-score 1.00
• P23176 · AlphaFold monomer V2.0 prediction for glucoamylase I (P23176) · 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 P23176
• Elsewhere: RCSB PDB 1AGM · PDBe 1AGM · UniProt P23176