Structure of PDB 1gwt Chain A

Receptor sequence

>1gwtA (length=307) Species: 3704 (Armoracia rusticana)

MQLTPTFYDNSCPNVSNIVRDTIVNELRSDPRIAASILRLHFHDCFVNGC
DASILLDNTTSFRTEKDAFGNANSARGFPVIDRMKAAVESACPRTVSCAD
LLTIAAQQSVTLAGGPSWRVPLGRRDSLQAFLDLANANLPAPFFTLPQLK
DSFRNVGLNRSSDLVALSGGHTFGKNQCRFIMDRLYNFSNTGLPDPTLNT
TYLQTLRGLCPLNGNLSALVDMDLRTPTIFDNKYYVNLEEQKGLIQSDQE
LFSSPNATDTIPLVRSFANSTQTFFNAFVEAMDRMGNITPLTGTQGQIRL
NCRVVNS

3D structure

• PDB: 1gwt 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: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R38 H42 N70 H170
• Catalytic site (residue number reindexed from 1): R39 H43 N71 H171
• 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 L166 H170 G173 N175 Q176 F179 M221 S306	R32 A35 S36 R39 F42 S74 P140 A141 P142 L167 H171 G174 N176 Q177 F180 M222 S307
BS02	CA	A	D43 V46 G48 D50 S52	D44 V47 G49 D51 S53
BS03	CA	A	T171 D222 T225 I228 D230	T172 D223 T226 I229 D231

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:1gwt, PDBe:1gwt, PDBj:1gwt
• PDBsum: 1gwt
• UniProt: P00433|PER1A_ARMRU Peroxidase C1A (Gene Name=PRXC1A)