X-ray diffraction
1.66Å 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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 524 amino acids
Theoretical weight: 58.49 KDa
Source organism: Ruminococcus bromii
Expression system: Escherichia coli
  • Canonical: A0A2N0UXJ4 (Residues: 28-551; Coverage: 100%)
Gene name: RBL236_00453
Sequence domains: Alpha amylase, catalytic domain

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P41212
Unit cell:
a: 98.46Å b: 98.46Å c: 196.22Å
α: 90° β: 90° γ: 90°
R R work R free
0.161 0.16 0.181
Expression system: Escherichia coli