Structure of PDB 4au9 Chain A

Receptor sequence
>4au9A (length=448) Species: 29892 (Auricularia auricula-judae) [Search protein sequence]
ATSLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTFLASDIAPVVASV
TQLSNVATQPLVALNIAFSNTGLLALGVTDNLGDSLFANGQAKDATSFKE
STSSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLS
ASIRPGNEAGHEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATND
PITRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQARADLLGA
RMVGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCP
FSAHIRKTRPRADLGGSLTPPNLSAGANSIMRSGIPYGPEVTSAESASNT
TTQERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQ
NNGQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA
3D structure
PDB4au9 First Crystal Structure of a Fungal High-Redox Potential Dye-Decolorizing Peroxidase: Substrate Interaction Sites and Long-Range Electron Transfer.
ChainA
Resolution2.1 Å
3D
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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 D168 G169 I170 A171 Q221 R255 H304 I305 T308 R309 R332 F359 I398 D168 G169 I170 A171 Q221 R255 H304 I305 T308 R309 R332 F359 I398
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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Cellular Component
External links
PDB RCSB:4au9, PDBe:4au9, PDBj:4au9
PDBsum4au9
PubMed23235158
UniProtI2DBY1|DYP_AURAJ Dye-decolorizing peroxidase AauDyP1 (Gene Name=dyp1)

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