Structure of PDB 5fnb Chain B

Receptor sequence

>5fnbB (length=315) Species: 5323 (Pleurotus eryngii)

ATCDDGRTTANAACCILFPILDDIQENLFDGAQCGEKVRESLRLTFHDAI
GFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAG
DFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILA
RMGDAGFSPAEVVWLLASHSIAAAGMPFDSTPGVFDSQFFIETLLKGRLN
KGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSK
MALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLSDVEQACAATPFPA
LTADPGPVTSVPPVP

3D structure

• PDB: 5fnb Unveiling the Basis of Alkaline Stability of an Evolved Versatile Peroxidase.
• Chain: B
• 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 F178 D217
• 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	B	D48 G60 D62 S64	D48 G60 D62 S64
BS02	CA	B	S170 D187 T189 V192 D194	S170 D179 T181 V184 D186
BS03	HEM	B	R39 E40 L42 R43 F46 P141 S168 H169 A172 A173 A174 F186 L228	R39 E40 L42 R43 F46 P141 S168 H169 A172 A173 A174 F178 L214

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)