1ht6

X-ray diffraction
1.5Å resolution

CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1

Released:

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 44.64 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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P21212
Unit cell:
a: 88.36Å b: 72.82Å c: 61.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.136 0.136 0.163
Expression system: Komagataella pastoris