PDBe 3eqa

X-ray diffraction
1.9Å resolution

Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol

Released:
Source organism: Aspergillus niger
Primary publication:
Structure of the catalytic domain of glucoamylase from Aspergillus niger.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 67 188-92 (2011)
PMID: 21301084

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: 50.5 KDa
Source organism: Aspergillus niger
UniProt:
  • Canonical: P69328 (Residues: 25-494; Coverage: 76%)
Gene name: GLAA
Sequence domains: Glycosyl hydrolases family 15
Structure domains: Glycosyltransferase

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P212121
Unit cell:
a: 57.826Å b: 73.222Å c: 106.793Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.181 0.229