PDBe 1gcy

X-ray diffraction
1.6Å resolution

HIGH RESOLUTION CRYSTAL STRUCTURE OF MALTOTETRAOSE-FORMING EXO-AMYLASE

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucan 1,4-alpha-maltotetraohydrolase Chain: A
Molecule details ›
Chain: A
Length: 527 amino acids
Theoretical weight: 57.77 KDa
Source organism: Pseudomonas stutzeri
Expression system: Escherichia coli
UniProt:
  • Canonical: P13507 (Residues: 22-548; Coverage: 100%)
Gene name: amyP
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL24XU
Spacegroup: P212121
Unit cell:
a: 69.42Å b: 171.66Å c: 46.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.259 0.259 0.304
Expression system: Escherichia coli