› 3bsg

X-ray diffraction
1.95Å resolution

Barley alpha-amylase isozyme 1 (AMY1) H395A mutant

Released:
DOI: 10.2210/pdb3bsg/pdb
PDB entry 3bsg coloured by chain, front view.
PDB entry 3bsg coloured by chain, side view.
PDB entry 3bsg coloured by chain, top view.
Source organism: Hordeum vulgare
Primary publication:
Multi-site substrate binding and interplay in barley alpha-amylase 1.
Nielsen MM, Seo ES, Bozonnet S, Aghajari N, Robert X, Haser R, Svensson B
FEBS Lett 582 2567-71 (2008)
PMID: 18588886

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: 414 amino acids
Theoretical weight: 45.43 KDa
Source organism: Hordeum vulgare
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P00693 (Residues: 25-438; Coverage: 100%)
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 ID14-1
Spacegroup: P21212
Unit cell:
a: 91.15Å b: 72.23Å c: 61.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.211 0.266
Expression system: Komagataella pastoris

Quick links

Citations

4 review citations

The carbohydrate-binding module family 20--diversity, structure, and function.
Christiansen et al. (2009)
3 more