Literature summary for 1.11.1.19 extracted from

Strittmatter, E.; Liers, C.; Ullrich, R.; Wachter, S.; Hofrichter, M.; Plattner, D.A.; Piontek, K.
First crystal structure of a fungal high-redox potential dye-decolorizing peroxidase: substrate interaction sites and long-range electron transfer (2013), J. Biol. Chem., 288, 4095-4102.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
to 2.1 A resolution. At the distal side of the heme molecule, flexible aspartate residue Asp168 plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterward, its side chain changes its conformation, now pointing toward the protein backbone. A transient radical on the surface-exposed residue Tyr337 is the oxidation site for bulky substrates	Auricularia auricula-judae

Crystallization (Comment)

Organism

to 2.1 A resolution. At the distal side of the heme molecule, flexible aspartate residue Asp168 plays a key role in catalysis. It guides incoming hydrogen peroxide toward the heme iron and mediates proton rearrangement in the process of Compound I formation. Afterward, its side chain changes its conformation, now pointing toward the protein backbone. A transient radical on the surface-exposed residue Tyr337 is the oxidation site for bulky substrates

Auricularia auricula-judae

Organism

Organism	UniProt	Comment	Textmining
Auricularia auricula-judae	I2DBY1	-	-

Cofactor

Cofactor	Comment	Organism	Structure
heme	-	Auricularia auricula-judae

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Release 2026.1 (March 2026)