PDBe 1jd9

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE ANALYSIS OF THE MUTANT K300Q OF PSEUDOALTEROMONAS HALOPLANCTIS ALPHA-AMYLASE

Released:
Primary publication:
Structural basis of alpha-amylase activation by chloride.
Protein Sci. 11 1435-41 (2002)
PMID: 12021442

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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2221
Unit cell:
a: 71.5Å b: 138.4Å c: 115.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.245
Expression system: Escherichia coli