Structure of PDB 1lyk Chain B

Receptor sequence

>1lykB (length=336) Species: 5346 (Coprinopsis cinerea)

SVTCPGGQSTSNSQCCVWFDVLDDLQTNFYQGSKCESPVRKILRIVFHDA
IGFSPALTAAGQFGGGGADGSIIAHSNIELAFPANGGLTDTVEALRAVGI
NHGVSFGDLIQFATAVGMSNCPGSPRLEFLTGRSNSSQPSPPSLIPGPGN
TVTAILDRMGDAGFSPDEVVDLLAAHSLASQEGLNSAIFRSPLDSTPQVF
DTQFYIETLLKGTTQPGPSLGFAEELSPFPGEFRMRSDALLARDSRTACR
WQSMTSSNEVMGQRYRAAMAKMSVLGFDRNALTDCSDVIPSAVSNNAAPV
IPGGLTVDDIEVSCPSEPFPEIATASGPLPSLAPAP

3D structure

• PDB: 1lyk Impact of the physical and chemical environment on the molecular structure of Coprinus cinereus peroxidase.
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R51 H55 H183 L200
• 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	MAN	B	S338 L339	S331 L332
BS02	CA	B	D56 G74 D76 S78	D49 G67 D69 S71
BS03	CA	B	S184 D201 T203 V206 D208	S177 D194 T196 V199 D201
BS04	HEM	B	R47 L50 R51 F54 G154 P155 L180 A182 H183 A186 S187 E189 G190 M242	R40 L43 R44 F47 G147 P148 L173 A175 H176 A179 S180 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:1lyk, PDBe:1lyk, PDBj:1lyk
• PDBsum: 1lyk
• PubMed: 12777760
• UniProt: P28314|PER_COPCI Peroxidase (Gene Name=CIP1)