Structure of PDB 6atj Chain A

Receptor sequence

>6atjA (length=306) Species: 3704 (Armoracia rusticana)

QLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGCD
ASILLDNTTSFRTEKDAFGNANSARGFPVIDRMKAAVESACPRTVSCADL
LTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLKD
SFRNVGLNRSSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNTT
YLQTLRGLCPLNGNLSALVDFDLRTPTIFDNKYYVNLEEQKGLIQSDQEL
FSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRLN
CRVVNS

3D structure

• PDB: 6atj The structures of the horseradish peroxidase C-ferulic acid complex and the ternary complex with cyanide suggest how peroxidases oxidize small phenolic substrates.
• Chain: A
• Resolution: 2.0 Å

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	CA	A	D43 V46 G48 D50 S52	D43 V46 G48 D50 S52
BS02	CA	A	T171 D222 T225 I228 D230	T171 D222 T225 I228 D230
BS03	HEM	A	R31 A34 S35 L37 R38 F41 S73 P139 A140 P141 L166 H170 G173 K174 N175 Q176 F179 F221	R31 A34 S35 L37 R38 F41 S73 P139 A140 P141 L166 H170 G173 K174 N175 Q176 F179 F221
BS04	FER	A	F68 G69 A140	F68 G69 A140

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

External links

• PDB: RCSB:6atj, PDBe:6atj, PDBj:6atj
• PDBsum: 6atj
• PubMed: 10574977
• UniProt: P00433|PER1A_ARMRU Peroxidase C1A (Gene Name=PRXC1A)