Structure of PDB 1arp Chain A

Receptor sequence

>1arpA (length=336) Species: 5079 (Penicillium janthinellum)

SVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDA
IGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTIEALRAVGI
NHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGN
TVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVF
DTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACR
WQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPV
IPGGLTVDDIEVSCPSEPFPEIATASGPLPSLAPAP

3D structure

• PDB: 1arp Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 A resolution. Structural comparisons with the lignin and cytochrome c peroxidases.
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R52 H56 H184 L201
• Catalytic site (residue number reindexed from 1): R44 H48 H176 L193
• 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	D57 G75 D77 S79	D49 G67 D69 S71
BS02	CA	A	S185 D202 T204 V207 D209	S177 D194 T196 V199 D201
BS03	HEM	A	R48 L51 R52 F55 G155 P156 L181 A183 H184 A187 S188 Q189 E190 G191 M243	R40 L43 R44 F47 G147 P148 L173 A175 H176 A179 S180 Q181 E182 G183 M235

Gene Ontology

Molecular Function

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

Biological Process

• GO:0000302 response to reactive oxygen species
• GO:0006979 response to oxidative stress
• GO:0034599 cellular response to oxidative stress
• GO:0042744 hydrogen peroxide catabolic process
• GO:0098869 cellular oxidant detoxification

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:1arp, PDBe:1arp, PDBj:1arp
• PDBsum: 1arp
• PubMed: 8289254
• UniProt: P28313|PER_ARTRA Peroxidase