9H1M
Recombinant ferric horseradish peroxidase C1A
Summary for 9H1M
| Entry DOI | 10.2210/pdb9h1m/pdb |
| Descriptor | Peroxidase C1A, PROTOPORPHYRIN IX CONTAINING FE, CALCIUM ION, ... (6 entities in total) |
| Functional Keywords | horseradish peroxidase, ferric, oxidoreductases, heme, oxidoreductase |
| Biological source | Armoracia rusticana |
| Total number of polymer chains | 1 |
| Total formula weight | 35183.31 |
| Authors | Nesa, M.L.,Mandal, S.K.,Toelzer, C.,Humer, D.,Moody, P.C.E.,Berger, I.,Spadiut, O.,Raven, E.L. (deposition date: 2024-10-09, release date: 2025-03-19, Last modification date: 2025-04-16) |
| Primary citation | Nesa, M.L.,Mandal, S.K.,Toelzer, C.,Humer, D.,Moody, P.C.E.,Berger, I.,Spadiut, O.,Raven, E.L. Crystal structure of ferric recombinant horseradish peroxidase. J.Biol.Inorg.Chem., 30:221-227, 2025 Cited by PubMed Abstract: Horseradish peroxidase (HRP), isolated from horseradish roots, is heavily glycosylated, making it difficult to crystallize. In this work, we produced recombinant HRP in E. coli and obtained an X-ray structure of the ferric enzyme at 1.63 Å resolution. The structure shows that the recombinant HRP contains four disulphide bonds and two calcium ions, which are highly conserved in class III peroxidase enzymes. The heme active site contains histidine residues at the proximal (His 170) and distal (His 42) positions, and an active site arginine (Arg 38). Surprisingly, an ethylene glycol molecule was identified in the active site, forming hydrogen bonds with His 42 and Arg 38 at the δ-heme edge. The high yields obtained from the recombinant expression system, and the successful crystallization of the enzyme pave the way for new structural studies in the future. PubMed: 40053124DOI: 10.1007/s00775-025-02103-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.63 Å) |
Structure validation
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