Structure of PDB 5abq Chain A

Receptor sequence
>5abqA (length=312) Species: 5323 (Pleurotus eryngii) [Search protein sequence]
CDDGRTTANAACCILFPILDDIQENLFDGAQCGEEVHESLRLTFHDCIGF
SPTLGGGGCDGSIIAFSDIETNFPANAGIDEIVEAQKPFVAKHNISAGDF
IQFAGAVGVSNCPGGVRIPFFLGRPDAVKASPDHLVPEPFDSVTSILARM
GDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETL
LKGRLFPGTADNKGEAQSPLQGEIRLQSDELLARDPRTACEWQSMVNNQP
KIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLKD
VEQACRKTPFPR
3D structure
PDB5abq Improving the Ph-Stability of Versatile Peroxidase by Comparative Structural Analysis with a Naturally-Stable Manganese Peroxidase.
ChainA
Resolution2.293 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R43 H47 H169 F186 D231
Catalytic site (residue number reindexed from 1) R41 H45 H167 F184 D229
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5abq, PDBe:5abq, PDBj:5abq
PDBsum5abq
PubMed26496708
UniProtO94753|VPL2_PLEER Versatile peroxidase VPL2 (Gene Name=vpl2)

[Back to BioLiP]