Structure of PDB 1h55 Chain A Binding Site BS04

Receptor Information
>1h55 Chain A (length=306) Species: 3704 (Armoracia rusticana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCD
ASILLDNTTSFRTEKDAFGNANSARGFPVIDRMKAAVESACPRTVSCADL
LTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKD
SFRNVGLNRSSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTT
YLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQKGLIQSDQEL
FSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLN
CRVVNS
Ligand information
Ligand IDO
InChIInChI=1S/H2O/h1H2
InChIKeyXLYOFNOQVPJJNP-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		O
CACTVS 3.341[O]
FormulaO
NameOXYGEN ATOM
ChEMBLCHEMBL1098659
DrugBankDB09145
ZINC
PDB chain1h55 Chain A Residue 500 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1h55 The Catalytic Pathway of Horseradish Peroxidase at High Resolution
Resolution1.61 Å
Binding residue
(original residue number in PDB)		R38 F41
Binding residue
(residue number reindexed from 1)		R38 F41
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R38 H42 N70 H170
Catalytic site (residue number reindexed from 1) R38 H42 N70 H170
Enzyme Commision number 1.11.1.7: peroxidase.
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0140825 lactoperoxidase activity
Biological Process
GO:0006979 response to oxidative stress
GO:0042744 hydrogen peroxide catabolic process
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005576 extracellular region
GO:0005773 vacuole

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1h55, PDBe:1h55, PDBj:1h55
PDBsum1h55
PubMed12024218
UniProtP00433|PER1A_ARMRU Peroxidase C1A (Gene Name=PRXC1A)

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