PDBe 1jdd

X-ray diffraction
1.9Å resolution

MUTANT (E219Q) MALTOTETRAOSE-FORMING EXO-AMYLASE COCRYSTALLIZED WITH MALTOTETRAOSE (CRYSTAL TYPE 2)

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:
  • not assigned

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: 429 amino acids
Theoretical weight: 47.41 KDa
Source organism: Pseudomonas stutzeri
Expression system: Escherichia coli
UniProt:
  • Canonical: P13507 (Residues: 22-450; Coverage: 81%)
Gene name: amyP
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 65.6Å b: 170.7Å c: 46.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.191 not available
Expression system: Escherichia coli