5ABN

CRYSTAL STRUCTURE ANALYSIS OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII. MUTANT VPi. MUTATED RESIDUES D69S, T70D, S86E, D146T, Q202L, H232E, Q239R AND S301K.

Summary for 5ABN

• Entry DOI: 10.2210/pdb5abn/pdb
• Related: 5ABO 5ABQ
• Descriptor: VERSATILE PEROXIDASE VPL2, CALCIUM ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: class ii (fungal) peroxidases, protoporphyrin ix, electron transfer, lignin peroxidase, lignin degradation, manganese peroxidase, mn-independent oxidation phenolic non-phenolic aromatics, mnii oxidation, peroxidase, polyvalent peroxidase, oxidoreductase, heme, hydrogen peroxide, iron, manganese, metal-binding, secreted, zymogen
• Biological source: PLEUROTUS ERYNGII (BOLETUS OF THE STEPPES)
• Cellular location: Secreted : O94753
• Total number of polymer chains: 1
• Total formula weight: 35412.14

Authors

Medrano, F.J.,Romero, A. (deposition date: 2015-08-07, release date: 2015-11-04, Last modification date: 2024-01-10)

• Primary citation: Saez-Jimenez, V.,Fernendez-Fueyo, E.,Medrano, F.J.,Romero, A.,Martinez, A.T.,Ruiz-Duenas, F.J.; Improving the Ph-Stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase.; Plos One, 10:40984-, 2015; PubMed: 26496708; DOI: 10.1371/JOURNAL.PONE.0140984

Experimental method

X-RAY DIFFRACTION (2.194 Å)