2d3l

X-ray diffraction
2.3Å resolution

Crystal structure of maltohexaose-producing amylase from Bacillus sp.707 complexed with maltopentaose.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148647 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Glucan 1,4-alpha-maltohexaosidase Chain: A
Molecule details ›
Chain: A
Length: 485 amino acids
Theoretical weight: 55.44 KDa
Source organism: Bacillus sp. 707
Expression system: Bacillus subtilis
UniProt:
  • Canonical: P19571 (Residues: 34-518; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer : NEW Components: GLC
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: P212121
Unit cell:
a: 47.45Å b: 82.46Å c: 126.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 0.213
Expression system: Bacillus subtilis