› 4w7l

X-ray diffraction
1.05Å resolution

CRYSTAL STRUCTURE OF A DECOLORIZING PEROXIDASE (DYP) FROM AURICULARIA AURICULA-JUDAE. D168N MUTANT

Released:
DOI: 10.2210/pdb4w7l/pdb
PDB entry 4w7l coloured by chain, front view.
PDB entry 4w7l coloured by chain, side view.
PDB entry 4w7l coloured by chain, top view.
Source organism: Auricularia auricula-judae
Primary publication:
Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study.
Linde D, Pogni R, Cañellas M, Lucas F, Guallar V, Baratto MC, Sinicropi A, Sáez-Jiménez V, Coscolín C, Romero A, Medrano FJ, Ruiz-Dueñas FJ, Martínez AT
OpenAccess logo Biochem J 466 253-62 (2015)
PMID: 25495127

Function and Biology Details

Reactions catalysed: 
Reactive Blue 5 + 2 H(2)O(2) = phthalate + 2,2'-disulfonyl azobenzene + 3-((4-amino-6-chloro-1,3,5-triazin-2-yl)amino)benzenesulfonate + 2 H(2)O
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125050 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dye-decolorizing peroxidase AauDyP1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 449 amino acids
Theoretical weight: 47.11 KDa
Source organism: Auricularia auricula-judae
Expression system: Escherichia coli
UniProt:
  • Canonical: I2DBY1 (Residues: 62-509; Coverage: 92%)
Gene name: dyp1
Sequence domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: C2
Unit cell:
a: 183.65Å b: 56.26Å c: 103.82Å
α: 90° β: 117.81° γ: 90°
R-values:
R R work R free
0.132 0.131 0.15
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Oxidoreductases on their way to industrial biotransformations.
Martínez et al. (2017)
5 more

4 mentions without citation

Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeIV = O formation in bacterial dye-decolorizing peroxidases.
Lučić et al. (2021)
3 more