7D8M

Crystal structure of DyP

Summary for 7D8M

Entry DOI	10.2210/pdb7d8m/pdb
Descriptor	Dye-decolorizing peroxidase, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (4 entities in total)
Functional Keywords	dye-decolorizing peroxidase, oxidoreductase
Biological source	Irpex lacteus (Milk-white toothed polypore)
Total number of polymer chains	1
Total formula weight	50691.47
Authors	He, C.,Jia, R.,Wang, T.,Li, L.Q. (deposition date: 2020-10-08, release date: 2021-08-18, Last modification date: 2023-11-29)
Primary citation	Li, L.,Wang, T.,Chen, T.,Huang, W.,Zhang, Y.,Jia, R.,He, C. Revealing two important tryptophan residues with completely different roles in a dye-decolorizing peroxidase from Irpex lacteus F17. Biotechnol Biofuels, 14:128-128, 2021 Cited by PubMed Abstract: Dye-decolorizing peroxidases (DyPs) represent a novel family of heme peroxidases that use HO as the final electron acceptor to catalyze the oxidation of various organic compounds. A DyP from Irpex lacteus F17 (Il-DyP4, corresponding to GenBank MG209114), obtained by heterologous expression, exhibits a high catalytic efficiency for phenolic compounds and a strong decolorizing ability toward various synthetic dyes. However, the enzyme structure and the catalytic residues involved in substrate oxidation remain poorly understood. PubMed: 34059116 DOI: 10.1186/s13068-021-01978-y PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2 Å)

Structure validation