PDBe 1aqm

X-ray diffraction
1.85Å resolution

ALPHA-AMYLASE FROM ALTEROMONAS HALOPLANCTIS COMPLEXED WITH TRIS

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-amylase Chain: A
Molecule details ›
Chain: A
Length: 453 amino acids
Theoretical weight: 49.38 KDa
Source organism: Pseudoalteromonas haloplanktis
Expression system: Escherichia coli
UniProt:
  • Canonical: P29957 (Residues: 25-477; Coverage: 70%)
Gene name: amy
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: C2221
Unit cell:
a: 71.4Å b: 138.9Å c: 115.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.157 0.186
Expression system: Escherichia coli