› 3fdy

X-ray diffraction
1.55Å resolution

Pyranose 2-oxidase thermostable triple mutant, T169G/E542K/V546C

Released:
DOI: 10.2210/pdb3fdy/pdb
PDB entry 3fdy coloured by chain, front view.
PDB entry 3fdy coloured by chain, side view.
PDB entry 3fdy coloured by chain, top view.
Source organism: Trametes ochracea
Primary publication:
A thermostable triple mutant of pyranose 2-oxidase from Trametes multicolor with improved properties for biotechnological applications.
Spadiut O, Radakovits K, Pisanelli I, Salaheddin C, Yamabhai M, Tan TC, Divne C, Haltrich D
Biotechnol J 4 525-34 (2009)
PMID: 19291706

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 Chain: A
Molecule details ›
Chain: A
Length: 623 amino acids
Theoretical weight: 69.37 KDa
Source organism: Trametes ochracea
Expression system: Escherichia coli BL21(DE3)
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 1 x FAD
1 bound ligand:
Ligand MES 1 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P42212
Unit cell:
a: 101.58Å b: 101.58Å c: 126.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.219
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

From protein engineering to immobilization: promising strategies for the upgrade of industrial enzymes.
Singh et al. (2013)
12 other articles