› 3lsi

X-ray diffraction
1.9Å resolution

Pyranose 2-oxidase T169A, tetragonal

Released:
DOI: 10.2210/pdb3lsi/pdb
Model geometry
Fit model/data
PDB entry 3lsi coloured by chain, front view.
PDB entry 3lsi coloured by chain, side view.
PDB entry 3lsi coloured by chain, top view.
Source organism: Trametes ochracea
Primary publication:
H-bonding and positive charge at the N5/O4 locus are critical for covalent flavin attachment in trametes pyranose 2-oxidase.
Tan TC, Pitsawong W, Wongnate T, Spadiut O, Haltrich D, Chaiyen P, Divne C
J Mol Biol 402 578-94 (2010)
PMID: 20708626

Function and Biology Details

Reaction catalysed: 
D-glucose + O(2) = 2-dehydro-D-glucose + H(2)O(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182318 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyranose 2-oxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 623 amino acids
Theoretical weight: 69.38 KDa
Source organism: Trametes ochracea
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7ZA32 (Residues: 1-623; Coverage: 100%)
Gene name: p2o
Sequence domains: GMC oxidoreductase
Structure domains: Phage tail proteins - 2 layer sandwich fold

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P43212
Unit cell:
a: 101.298Å b: 101.298Å c: 249.768Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.213
Expression system: Escherichia coli

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Citations

1 review citation

The substrate oxidation mechanism of pyranose 2-oxidase and other related enzymes in the glucose-methanol-choline superfamily.
Wongnate et al. (2013)
14 other articles