Structure of PDB 1w4w Chain A

Receptor sequence
>1w4wA (length=306) Species: 3704 (Armoracia rusticana) [Search protein sequence]
QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCD
ASILLDNTTSFRTEKDAFGNANSARGFPVIDRMKAAVESACPRTVSCADL
LTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKD
SFRNVGLNRSSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTT
YLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQKGLIQSDQEL
FSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLN
CRVVNS
3D structure
PDB1w4w Complexes of Horseradish Peroxidase with Formate, Acetate, and Carbon Monoxide
ChainA
Resolution1.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 R31 A34 S35 R38 F41 S73 P139 A140 P141 L148 L166 H170 G173 N175 Q176 F179 F221 R31 A34 S35 R38 F41 S73 P139 A140 P141 L148 L166 H170 G173 N175 Q176 F179 F221
BS02 CA A D43 V46 G48 D50 S52 D43 V46 G48 D50 S52
BS03 CA A T171 D222 T225 I228 D230 T171 D222 T225 I228 D230
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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Cellular Component
External links
PDB RCSB:1w4w, PDBe:1w4w, PDBj:1w4w
PDBsum1w4w
PubMed15641789
UniProtP00433|PER1A_ARMRU Peroxidase C1A (Gene Name=PRXC1A)

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