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 | UniProt | Comment | Textmining |
---|---|---|---|
Auricularia auricula-judae | I2DBY1 | - |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
heme | - |
Auricularia auricula-judae |