PDBe 3gly

X-ray diffraction
2.2Å resolution

REFINED CRYSTAL STRUCTURES OF GLUCOAMYLASE FROM ASPERGILLUS AWAMORI VAR. X100

Released:
Source organism: Aspergillus awamori

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D- glucose. 
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucoamylase Chain: A
Molecule details ›
Chain: A
Length: 470 amino acids
Theoretical weight: 50.45 KDa
Source organism: Aspergillus awamori
Expression system: Not provided
UniProt:
  • Canonical: P69327 (Residues: 25-495; Coverage: 76%)
Gene name: GLAA
Structure domains: Glycosyltransferase

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 116.7Å b: 104.3Å c: 48.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 not available not available
Expression system: Not provided