Structure of PDB 1llp Chain A

Receptor sequence
>1llpA (length=343) [Search protein sequence]
ATCANGKTVGDASCCAWFDVLDDIQANMFHGGQCGAEAHESIRLVFHDSI
AISPAMEAKGKFGGGGADGSIMIFDTIETAFHPNIGLDEVVAMQKPFVQK
HGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRKPATQPAPDGLVPEPFHT
VDQIIARVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGIF
DSQFFVETQFRGTLFPGSGGNQGEVESGMAGEIRIQTDHTLARDSRTACE
WQSFVGNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPLSKPIPGNGP
FSFFPPGKSHSDIEQACAETPFPSLVTLPGPATSVARIPPHKA
3D structure
PDB1llp The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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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
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1llp, PDBe:1llp, PDBj:1llp
PDBsum1llp
PubMed10024453
UniProtP49012|LIG2_PHACH Ligninase LG2 (Gene Name=GLG2)

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