› 4mig

X-ray diffraction
1.8Å resolution

Pyranose 2-oxidase from Phanerochaete chrysosporium, recombinant wild type

Released:
DOI: 10.2210/pdb4mig/pdb
PDB entry 4mig coloured by chain, front view.
PDB entry 4mig coloured by chain, side view.
PDB entry 4mig coloured by chain, top view.
Source organism: Phanerodontia chrysosporium
Primary publication:
Crystal structures of Phanerochaete chrysosporium pyranose 2-oxidase suggest that the N-terminus acts as a propeptide that assists in homotetramer assembly.
Hassan N, Tan TC, Spadiut O, Pisanelli I, Fusco L, Haltrich D, Peterbauer CK, Divne C
OpenAccess logo FEBS Open Bio 3 496-504 (2013)
PMID: 24282677

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-180283 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyranose 2-oxidase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 648 amino acids
Theoretical weight: 72.29 KDa
Source organism: Phanerodontia chrysosporium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6QWR1 (Residues: 1-621; Coverage: 100%)
Gene names: p2ox, pox
Sequence domains: GMC oxidoreductase

Ligands and Environments


Cofactor: Ligand FDA 4 x FDA
2 bound ligands:
Ligand G3F 4 x G3F
Ligand MN 8 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P21
Unit cell:
a: 89.544Å b: 166.448Å c: 91.844Å
α: 90° β: 106.41° γ: 90°
R-values:
R R work R free
0.174 0.173 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Multiplicity of enzymatic functions in the CAZy AA3 family.
Sützl et al. (2018)
7 other articles

2 mentions without citation

Crystal structures of Phanerochaete chrysosporium pyranose 2-oxidase suggest that the N-terminus acts as a propeptide that assists in homotetramer assembly.
Hassan et al. (2013)
1 more