Structure of PDB 1qgj Chain B

Receptor sequence

>1qgjB (length=300) Species: 3702 (Arabidopsis thaliana)

QLSPDIYAKSCPNLVQIVRKQVAIALKAEIRMAASLIRLHFHDCFVNGCD
ASLLLDGADSEKLAIPNINSARGFEVIDTIKAAVENACPGVVSCADILTL
AARDSVVLSGGPGWRVALGRKDGLVANQNSANNLPSPFEPLDAIIAKFVA
VNLNITDVVALSGAHTFGQAKCAVFSNRLFNFTGAGNPDATLETSLLSNL
QTVCPLGGNSNITAPLDRSTTDTFDNNYFKNLLEGKGLLSSDQILFSSDL
AVNTTKKLVEAYSRSQSLFFRDFTCAMIRMGNISNGASGEVRTNCRVINN

3D structure

• PDB: 1qgj Arabidopsis thaliana peroxidase N: structure of a novel neutral peroxidase.
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R38 H42 N67 H165
• Catalytic site (residue number reindexed from 1): R38 H42 N67 H165
• 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	B	D43 V46 G48 D50 S52	D43 V46 G48 D50 S52
BS02	CA	B	T166 D217 T220 T223 D225	T166 D217 T220 T223 D225
BS03	HEM	B	R31 A34 S35 R38 F41 S70 P135 S136 P137 A164 H165 G168 Q169 A170 K171 L216 L239 S241	R31 A34 S35 R38 F41 S70 P135 S136 P137 A164 H165 G168 Q169 A170 K171 L216 L239 S241
BS04	GSH	B	T156 C275 A276 R279	T156 C275 A276 R279

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:0005634 nucleus
• GO:0005737 cytoplasm

External links

• PDB: RCSB:1qgj, PDBe:1qgj, PDBj:1qgj
• PDBsum: 1qgj
• PubMed: 10713531
• UniProt: Q39034|PER59_ARATH Peroxidase 59 (Gene Name=PER59)