Structure of PDB 5ag1 Chain A

Receptor sequence
>5ag1A (length=446) Species: 29892 (Auricularia auricula-judae) [Search protein sequence]
SLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASVTQ
LSNVATQPLVALNIAFSNTGLLALGVTDNLGDSLFANGQAKDATSFKEST
SSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLSAS
IRPGNEAGHEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATNDPI
TRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQARADLLGARM
VGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCPFS
AHIRKTRPRADLGGSLTPPNLSAGANSIMRSGIPYGPEVTSAESASNTTT
QERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQNN
GQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA
3D structure
PDB5ag1 Crystallographic Trapping of a Covalently Modified Heme in a Dye-Decolorizing Peroxidase
ChainA
Resolution1.85 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 N7H A E162 D168 G169 I170 A171 L219 Q221 V253 R255 H304 I305 T308 R309 R332 L357 F359 F370 I398 E160 D166 G167 I168 A169 L217 Q219 V251 R253 H302 I303 T306 R307 R330 L355 F357 F368 I396
BS02 NO2 A R332 F359 R330 F357
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:5ag1, PDBe:5ag1, PDBj:5ag1
PDBsum5ag1
PubMed
UniProtI2DBY1|DYP_AURAJ Dye-decolorizing peroxidase AauDyP1 (Gene Name=dyp1)

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