Acarbose rearrangement mechanism implied by the kinetic and structural analysis of human pancreatic alpha-amylase in complex with analogues and their elongated counterparts

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 24% 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 · chains A
• BGC · beta-D-glucopyranose · sugar · chains A
• GLC · alpha-D-glucopyranose · sugar · 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

• 1XCX · Acarbose Rearrangement Mechanism Implied by the Kinetic and Structural Analysis of Human… · 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 1XCX · PDBe 1XCX · UniProt P04746