Structure of PDB 1pa2 Chain A

Receptor sequence

>1pa2A (length=306) Species: 3702 (Arabidopsis thaliana)

MQLNATFYSGTCPNASAIVRSTIQQALQSDTRIGASLIRLHFHDCFVNGC
DASILLDDTGSIQSEKNAGPNVNSARGFNVVDNIKTALENACPGVVSCSD
VLALASEASVSLAGGPSWTVLLGRRDSLTANLAGANSSIPSPIESLSNIT
FKFSAVGLNTNDLVALSGAHTFGRARCGVFNNRLFNFSGTGNPDPTLNST
LLSTLQQLCPQNGSASTITNLDLSTPDAFDNNYFANLQSNDGLLQSDQEL
FSTTGSSTIAIVTSFASNQTLFFQAFAQSMINMGNISPLTGSNGEIRLDC
KKVNGS

3D structure

• PDB: 1pa2 Arabidopsis ATP A2 peroxidase. Expression and high-resolution structure of a plant peroxidase with implications for lignification.
• Chain: A
• Resolution: 1.45 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R38 H42 N70 H169
• Catalytic site (residue number reindexed from 1): R39 H43 N71 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	D44 V47 G49 D51 S53
BS02	CA	A	T170 D221 T224 A227 D229	T171 D222 T225 A228 D230
BS03	HEM	A	R31 A34 S35 R38 F41 S73 P139 S140 P141 F152 A168 H169 G172 R173 A174 R175 L220 L243	R32 A35 S36 R39 F42 S74 P140 S141 P142 F153 A169 H170 G173 R174 A175 R176 L221 L244

Gene Ontology

Molecular Function

• GO:0004601 peroxidase activity
• GO:0020037 heme binding
• GO:0046872 metal ion binding
• GO:0140825 lactoperoxidase activity

Biological Process

• GO:0002215 defense response to nematode
• GO:0006979 response to oxidative stress
• GO:0009908 flower development
• GO:0042744 hydrogen peroxide catabolic process
• GO:0098869 cellular oxidant detoxification

Cellular Component

• GO:0005576 extracellular region
• GO:0005794 Golgi apparatus

External links

• PDB: RCSB:1pa2, PDBe:1pa2, PDBj:1pa2
• PDBsum: 1pa2
• PubMed: 11117266
• UniProt: Q42578|PER53_ARATH Peroxidase 53 (Gene Name=PER53)