PDBsum entry 1gal

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protein ligands links
Oxidoreductase(flavoprotein) PDB id
Jmol PyMol
Protein chain
581 a.a. *
NAG ×4
Waters ×152
* Residue conservation analysis
PDB id:
Name: Oxidoreductase(flavoprotein)
Title: Crystal structure of glucose oxidase from aspergillus niger: at 2.3 angstroms resolution
Structure: Glucose oxidase. Chain: a. Engineered: yes
Source: Aspergillus niger. Organism_taxid: 5061
2.30Å     R-factor:   0.181    
Authors: H.J.Hecht,K.Kalisz,J.Hendle,R.D.Schmid,D.Schomburg
Key ref: H.J.Hecht et al. (1993). Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution. J Mol Biol, 229, 153-172. PubMed id: 8421298
27-Aug-92     Release date:   31-Oct-93    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P13006  (GOX_ASPNG) -  Glucose oxidase
605 a.a.
581 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Glucose oxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Beta-D-glucose + O2 = D-glucono-1,5-lactone + H2O2
Bound ligand (Het Group name = BMA)
matches with 91.67% similarity
+ O(2)
= D-glucono-1,5-lactone
+ H(2)O(2)
      Cofactor: FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     oxidation-reduction process   1 term 
  Biochemical function     oxidoreductase activity     4 terms  


J Mol Biol 229:153-172 (1993)
PubMed id: 8421298  
Crystal structure of glucose oxidase from Aspergillus niger refined at 2.3 A resolution.
H.J.Hecht, H.M.Kalisz, J.Hendle, R.D.Schmid, D.Schomburg.
Glucose oxidase (beta-D-glucose: oxygen 1-oxidoreductase, EC is an FAD-dependent enzyme that catalyzes the oxidation of beta-D-glucose by molecular oxygen. The crystal structure of the partially deglycosylated enzyme from Aspergillus niger has been determined by isomorphous replacement and refined to 2.3 A resolution. The final crystallographic R-value is 18.1% for reflections between 10.0 and 2.3 A resolution. The refined model includes 580 amino acid residues, the FAD cofactor, six N-acetylglucosamine residues, three mannose residues and 152 solvent molecules. The FAD-binding domain is topologically very similar to other FAD-binding proteins. The substrate-binding domain is formed from non-continuous segments of sequence and is characterized by a deep pocket. One side of this pocket is formed by a six-stranded antiparallel beta-sheet with the flavin ring system of FAD located at the bottom of the pocket on the opposite side. Part of the entrance to the active site pocket is at the interface to the second subunit of the dimeric enzyme and is formed by a 20-residue lid, which in addition covers parts of the FAD-binding site. The carbohydrate moiety attached to Asn89 at the tip of this lid forms a link between the subunits of the dimer.

Literature references that cite this PDB file's key reference

  PubMed id Reference
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PDB code: 3fim
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PDB codes: 2jbr 2jbs 2jbt
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PDB code: 1naa
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Monovalent cation-induced conformational change in glucose oxidase leading to stabilization of the enzyme.
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Stability of crystalline proteins.
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PDB code: 1qjn
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PDB codes: 1f8r 1f8s
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Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family.
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PDB code: 1chu
10368296 C.Binda, A.Coda, R.Angelini, R.Federico, P.Ascenzi, and A.Mattevi (1999).
A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase.
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PDB codes: 1b37 1b5q
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Protein folding at the air-water interface studied with x-ray reflectivity.
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Modeling the surface phenomena in carbon paste electrodes by low frequency impedance and double-layer capacitance measurements.
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Imaging of biological macromolecules on mica in humid air by scanning electrochemical microscopy.
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1.8 and 1.9 A resolution structures of the Penicillium amagasakiense and Aspergillus niger glucose oxidases as a basis for modelling substrate complexes.
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PDB codes: 1cf3 1gpe
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Changes in secondary structure and salt links of cytochrome P-450cam induced by photoreduction: a Fourier transform infrared spectroscopic study.
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Second harmonic generation of glucose oxidase at the air/water interface.
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PDB code: 2gb0
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Crystal structure determination of cholesterol oxidase from Streptomyces and structural characterization of key active site mutants.
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PDB codes: 1b4v 1b8s 1cbo 1cc2
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PDB code: 1foh
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PDB code: 1alq
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PDB code: 1kif
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Crystal structure of NADH oxidase from Thermus thermophilus.
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PDB code: 1nox
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ESR and electron nuclear double resonance characterization of the cholesterol oxidase from Brevibacterium sterolicum in its semiquinone state.
  Eur J Biochem, 222, 941-947.  
18618774 P.Saudan, S.M.Zakeeruddin, M.A.Malavallon, M.Grätzel, and D.M.Fraser (1994).
Novel redox surfactants and their interactions with glucose oxidase of Aspergillus niger.
  Biotechnol Bioeng, 44, 407-418.  
  7756982 W.J.van Berkel, M.H.Eppink, and H.A.Schreuder (1994).
Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin.
  Protein Sci, 3, 2245-2253.
PDB code: 1pdh
8357574 H.J.Hecht, D.Schomburg, H.Kalisz, and R.D.Schmid (1993).
The 3D structure of glucose oxidase from Aspergillus niger. Implications for the use of GOD as a biosensor enzyme.
  Biosens Bioelectron, 8, 197-203.  
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