Structure of PDB 5fnb Chain A

Receptor sequence

>5fnbA (length=329) Species: 5323 (Pleurotus eryngii)

ATCDDGRTTANAACCILFPILDDIQENLFDGAQCGEKVRESLRLTFHDAI
GFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAG
DFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILA
RMGDAGFSPAEVVWLLASHSIAAADKVDPSIPGMPFDSTPGVFDSQFFIE
TLLKGRLFPGTAANKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNN
QPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSL
SDVEQACAATPFPALTADPGPVTSVPPVP

3D structure

• PDB: 5fnb Unveiling the Basis of Alkaline Stability of an Evolved Versatile Peroxidase.
• Chain: A
• Resolution: 1.792 Å

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

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	CA	A	D48 G60 D62 S64	D48 G60 D62 S64
BS02	CA	A	S170 D187 T189 V192 D194	S170 D187 T189 V192 D194
BS03	HEM	A	R39 L42 R43 F46 E140 P141 S168 H169 A172 A173 A174 D175 K176 V177 F186 L228	R39 L42 R43 F46 E140 P141 S168 H169 A172 A173 A174 D175 K176 V177 F186 L228

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

External links

• PDB: RCSB:5fnb, PDBe:5fnb, PDBj:5fnb
• PDBsum: 5fnb
• PubMed: 27118867
• UniProt: O94753|VPL2_PLEER Versatile peroxidase VPL2 (Gene Name=vpl2)