In situ extension as an approach for identifying novel alpha-amylase inhibitors, structure containing maltosyl-alpha (1,4)-D- gluconhydroximo-1,5-lactam

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 24% strand (DSSP).

Ligands and binding sites

• LAG · Maltosyl-alpha (1,4)-(Z,3S,4S,5R,6R)-3,4,5-trihydroxy-6-hydroxymethyl-piperidin-2-one oxime · ligand · chains A
• GOX · (2S,3S,4R,5R)-6-(hydroxyamino)-2-(hydroxymethyl)-2,3,4,5-tetrahydropyridine-3,4,5-triol · ligand · chains A
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
• CA · Calcium ion · metal · chains A
• CL · Chloride ion · ion · chains A

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

Pockets

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

Modifications

Observed in the structure: 5 disulfide, 1 glycan, 1 modified (disulfide, N-glycosylation, cyclization).

Compared structures

• 1U30 · In situ extension as an approach for identifying novel alpha-amylase inhibitors… · the same entry in another collection · chain A against A, TM-score 1.00
• P04746 · AlphaFold monomer V2.0 prediction for pancreatic alpha-amylase (P04746) · 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 P04746
• Elsewhere: RCSB PDB 1U30 · PDBe 1U30 · UniProt P04746