› 3old

X-ray diffraction
2Å resolution

Crystal structure of alpha-amylase in complex with acarviostatin I03

Released:
DOI: 10.2210/pdb3old/pdb
PDB entry 3old coloured by chain, front view.
PDB entry 3old coloured by chain, side view.
PDB entry 3old coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human pancreatic α-amylase in complex with acarviostatins: Implications for drug design against type II diabetes.
Qin X, Ren L, Yang X, Bai F, Wang L, Geng P, Bai G, Shen Y
J Struct Biol 174 196-202 (2011)
PMID: 21111049

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138163 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (5 distinct):
Pancreatic alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 496 amino acids
Theoretical weight: 55.98 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P04746 (Residues: 16-511; Coverage: 100%)
Gene name: AMY2A
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, G6D
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, BGC
Carbohydrate polymer
7 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
Ligand SO4 1 x SO4
Ligand NAG 1 x NAG
Ligand ACI 1 x ACI
Ligand PCA 1 x PCA
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BSRF BEAMLINE 1W2B
Spacegroup: P212121
Unit cell:
a: 51.986Å b: 67.76Å c: 130.469Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 0.194
Expression system: Saccharomyces cerevisiae

Quick links

Citations

6 review citations

α-Amylase: an enzyme specificity found in various families of glycoside hydrolases.
Janeček et al. (2014)
5 more

4 mentions without citation

Investigation on the Enzymatic Profile of Mulberry Alkaloids by Enzymatic Study and Molecular Docking.
Liu et al. (2019)
3 more