Structure of PDB 3fmu Chain A

Receptor sequence
>3fmuA (length=319) Species: 5323 (Pleurotus eryngii) [Search protein sequence]
ATCDDGRTTANAACCILFPILDDIQENLFDGAQCGEEVHESLRLTFHDAI
GFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAG
DFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILA
RMGDAGFSPVEVVSLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIE
TQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNN
QPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSL
SDVEQACAATPFPALTADP
3D structure
PDB3fmu Structural and Site-directed Mutagenesis Study of Versatile Peroxidase Oxidizing both Mn(II) and Aromatic Substrates
ChainA
Resolution1.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R43 H47 H169 F186 D231
Catalytic site (residue number reindexed from 1) R43 H47 H169 F186 D231
Enzyme Commision number 1.11.1.16: versatile peroxidase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016689 manganese peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0052750 reactive-black-5:hydrogen-peroxide oxidoreductase activity
Biological Process
GO:0000302 response to reactive oxygen species
GO:0006979 response to oxidative stress
GO:0034599 cellular response to oxidative stress
GO:0042744 hydrogen peroxide catabolic process
GO:0046274 lignin catabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region

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Cellular Component
External links
PDB RCSB:3fmu, PDBe:3fmu, PDBj:3fmu
PDBsum3fmu
PubMed
UniProtO94753|VPL2_PLEER Versatile peroxidase VPL2 (Gene Name=vpl2)

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