› 6frv

X-ray diffraction
2.3Å resolution

Structure of the catalytic domain of Aspergillus niger Glucoamylase

Released:
DOI: 10.2210/pdb6frv/pdb
PDB entry 6frv coloured by chain, front view.
PDB entry 6frv coloured by chain, side view.
PDB entry 6frv coloured by chain, top view.
Source organism: Aspergillus niger
Primary publication:
Structural insight into industrially relevant glucoamylases: flexible positions of starch-binding domains.
Roth C, Moroz OV, Ariza A, Skov LK, Ayabe K, Davies GJ, Wilson KS
Acta Crystallogr D Struct Biol 74 463-470 (2018)
PMID: 29717717

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159569 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glucoamylase Chain: A
Molecule details ›
Chain: A
Length: 616 amino acids
Theoretical weight: 65.82 KDa
Source organism: Aspergillus niger
Expression system: Aspergillus niger
UniProt:
  • Canonical: P69328 (Residues: 25-640; Coverage: 99%)
Gene name: GLAA
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
2 bound ligands:
Ligand NAG 1 x NAG
Ligand MAN 2 x MAN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 56.369Å b: 73.125Å c: 102.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.256 0.251 0.343
Expression system: Aspergillus niger

Quick links

Citations

2 review citations

Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms.
Sidar et al. (2020)
1 more

1 mention without citation

Crystal structure of TchmY from Actinoplanes teichomyceticus.
Yang et al. (2019)