Structure of PDB 1lga Chain B

Receptor sequence

>1lgaB (length=341)

ATCANGKTVGDASCCAWFDVLDDIQANMFHGGQCGAEAHESIRLVFHDSI
AISPAMEAKGKFGGGGADGSIMIFDTIETAFHPNIGLDEVVAMQKPFVQK
HGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRKPATQPAPDGLVPEPFHT
VDQIIARVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIF
DSQFFVETQFRGTLFPGSGGNQGEVESGMAGEIRIQTDHTLARDSRTACE
WQSFVGNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPLSKPIPGNGP
FSFFPPGKSHSDIEQACAETPFPSLVTLPGPATSVARIPPH

3D structure

• PDB: 1lga Crystallographic refinement of lignin peroxidase at 2 A.
• Chain: B
• Resolution: 2.03 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): H176 F193
• Catalytic site (residue number reindexed from 1): H176 F193
• Enzyme Commision number: 1.11.1.14: lignin 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	S177 D194 T196 I199 D201	S177 D194 T196 I199 D201
BS02	CA	B	D48 G66 D68 S70	D48 G66 D68 S70
BS03	HEM	B	H39 I42 R43 F46 E146 P147 M172 L173 A175 H176 A179 A180 V181 D183 F193	H39 I42 R43 F46 E146 P147 M172 L173 A175 H176 A179 A180 V181 D183 F193

Gene Ontology

Molecular Function

• GO:0004601 peroxidase activity
• GO:0016690 diarylpropane peroxidase activity
• GO:0020037 heme binding
• GO:0046872 metal ion binding

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:0046274 lignin catabolic process
• GO:0098869 cellular oxidant detoxification

External links

• PDB: RCSB:1lga, PDBe:1lga, PDBj:1lga
• PDBsum: 1lga
• PubMed: 8440725
• UniProt: P49012|LIG2_PHACH Ligninase LG2 (Gene Name=GLG2)