› 1cf3

X-ray diffraction
1.9Å resolution

GLUCOSE OXIDASE FROM APERGILLUS NIGER

Released:
DOI: 10.2210/pdb1cf3/pdb
PDB entry 1cf3 coloured by chain, front view.
PDB entry 1cf3 coloured by chain, side view.
PDB entry 1cf3 coloured by chain, top view.
Source organism: Aspergillus niger
Primary publication:
1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes.
Wohlfahrt G, Witt S, Hendle J, Schomburg D, Kalisz HM, Hecht HJ
Acta Crystallogr D Biol Crystallogr 55 969-77 (1999)
PMID: 10216293

Function and Biology Details

Reaction catalysed: 
Beta-D-glucose + O(2) = D-glucono-1,5-lactone + H(2)O(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glucose oxidase Chain: A
Molecule details ›
Chain: A
Length: 583 amino acids
Theoretical weight: 63.33 KDa
Source organism: Aspergillus niger
UniProt:
  • Canonical: P13006 (Residues: 23-605; Coverage: 100%)
Gene name: gox
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
1 bound ligand:
Ligand NAG 3 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P3121
Unit cell:
a: 67.54Å b: 67.54Å c: 215.38Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 0.24

Quick links

Citations

6 review citations

Sequence-structure analysis of FAD-containing proteins.
Dym et al. (2001)
5 more

47 mentions without citation

Review of glucose oxidases and glucose dehydrogenases: a bird's eye view of glucose sensing enzymes.
Ferri et al. (2011)
46 more