Structure of PDB 1b82 Chain A

Receptor sequence
>1b82A (length=349) [Search protein sequence]
VIEKRATCSNGKTVGDASCCAWFDVLDDIQQNLFHGGQCGAEAHESIRLV
FHDSIAISPAMEAQGKFGGGGADGSIMIFDDIETAFHPNIGLDEIVKLQK
PFVQKHGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRAPATQPAPDGLVP
EPFHTVDQIINRVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDS
TPGIFDSQFFVETQLRGTAFPGSGGNQGEVESPLPGEIRIQSDHTIARDS
RTACEWQSFVNNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPQSKPI
PGNLPFSFFPAGKTIKDVEQACAETPFPTLTTLPGPETSVQRIPPPPGA
3D structure
PDB1b82 Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.
ChainA
Resolution1.8 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) H181 F198
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 A D48 G66 D68 S70 D53 G71 D73 S75
BS02 CA A S177 D194 T196 I199 D201 S182 D199 T201 I204 D206
BS03 HEM A H39 R43 F46 E146 M172 L173 A175 H176 A179 A180 V181 D183 F193 H44 R48 F51 E151 M177 L178 A180 H181 A184 A185 V186 D188 F198
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:1b82, PDBe:1b82, PDBj:1b82
PDBsum1b82
PubMed11162097
UniProtP06181|LIG8_PHACH Ligninase H8 (Gene Name=LPOA)

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