Structure of PDB 5ag0 Chain B

Receptor sequence
>5ag0B (length=446) Species: 29892 (Auricularia auricula-judae) [Search protein sequence]
SLNTDDIQGDILVGMHKQKQLFYFFAINDPATFKTHLASDIAPVVASVTQ
LSNVATQPLVALNIAFSNTGLLALGVTDNLGDSLFANGQAKDATSFKEST
SSWVPQFAGTGIHGVIILASDTTDLIDQQVASIESTFGSSISKLYSLSAS
IRPGNEAGHEMFGFLDGIAQPAINGFNTPLPGQNIVDAGVIITGATNDPI
TRPSWAVGGSFLAFRQLEQLVPEFNKYLLDNAPAGSGSLQARADLLGARM
VGRWKSGAPIDLTPTADDPALGADAQRNNNFTYSHAGFDLGSDQSHCPFS
AHIRKTRPRADLGGSLTPPNLSAGANSIMRSGIPYGPEVTSAESASNTTT
QERGLAFVAYQAQLSQGFHFLQQTWADNANFPPGKTPATVGLDPIIGQNN
GQPRVVNGLLPSNSSASLSIPQFVVSHGGEYFFSPPISAIGGRLSA
3D structure
PDB5ag0 Crystallographic Trapping of a Covalently Modified Heme in a Dye-Decolorizing Peroxidase
ChainB
Resolution1.75 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 B D168 I170 A171 Q221 H304 I305 T308 R309 R332 L357 F359 I398 D166 I168 A169 Q219 H302 I303 T306 R307 R330 L355 F357 I396
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:5ag0, PDBe:5ag0, PDBj:5ag0
PDBsum5ag0
PubMed
UniProtI2DBY1|DYP_AURAJ Dye-decolorizing peroxidase AauDyP1 (Gene Name=dyp1)

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