› 2qpu

X-ray diffraction
1.7Å resolution

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132830 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-amylase type A isozyme Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 405 amino acids
Theoretical weight: 44.65 KDa
Source organism: Hordeum vulgare
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P00693 (Residues: 25-429; Coverage: 98%)
Gene name: AMY1.1
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: BGC, GLC, AC1
Ligand BGC 1 x BGC
Ligand GLC 1 x GLC
Ligand AC1 1 x AC1
4 bound ligands:
Ligand CA 12 x CA
Ligand EDO 2 x EDO
Ligand QPU 4 x QPU
Ligand BGC 1 x BGC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21212
Unit cell:
a: 218.93Å b: 89.65Å c: 62.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.209
Expression system: Komagataella pastoris

Quick links

Citations

11 review citations

Starch: its metabolism, evolution, and biotechnological modification in plants.
Zeeman et al. (2010)
10 more

1 mention without citation

New insights into the origin and evolution of α-amylase genes in green plants.
Ju et al. (2019)