› 2qps

X-ray diffraction
2.2Å 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
Macromolecule:
Alpha-amylase type A isozyme Chain: A
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 44.55 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

1 bound ligand:
Ligand CA 3 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21212
Unit cell:
a: 88.39Å b: 72.42Å c: 62.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.24 0.305
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