Structure of PDB 4w7l Chain A

Receptor sequence
>4w7lA (length=448) Species: 29892 (Auricularia auricula-judae) [Search protein sequence]
ATSLNTIDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASV
TQLSNVATQPLVALNIAFSNTGLLALGVTDNLGDSLFANGQAKDATSFKE
STSSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLS
ASIRPGNEAGHEMFGFLNGIAQPAINGFNTPLPGQNIVDAGVIITGATND
PITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQARADLLGA
RMVGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCP
FSAHIRKTRPRADLGGSLTPPNLSAGANSIMRSGIPYGPEVTSAESASNT
TTQERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQ
NNGQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA
3D structure
PDB4w7l Catalytic surface radical in dye-decolorizing peroxidase: a computational, spectroscopic and site-directed mutagenesis study.
ChainA
Resolution1.05 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.11.1.19: dye decolorizing peroxidase.
1.11.1.7: 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 HEM A E162 N168 G169 I170 A171 Q221 R255 H304 I305 T308 R309 R332 L357 F359 F370 I398 V426 E162 N168 G169 I170 A171 Q221 R255 H304 I305 T308 R309 R332 L357 F359 F370 I398 V426
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0140825 lactoperoxidase activity
Biological Process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4w7l, PDBe:4w7l, PDBj:4w7l
PDBsum4w7l
PubMed25495127
UniProtI2DBY1|DYP_AURAJ Dye-decolorizing peroxidase AauDyP1 (Gene Name=dyp1)

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