Structure of PDB 1b80 Chain B

Receptor sequence
>1b80B (length=345) [Search protein sequence]
RATCSNGKTVGDASCCAWFDVLDDIQQNLFHGGQCGAEAHESIRLVFHDS
IAISPAMEAQGKFGGGGADGSIMIFDDIETAFHPNIGLDEIVKLQKPFVQ
KHGVTPGDFIAFAGAVALSNCPGAPQMNFFTGRAPATQPAPDGLVPEPFH
TVDQIINRVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPGI
FDSQFFVETQLRGTAFPGSGGNQGEVESPLPGEIRIQSDHTIARDSRTAC
EWQSFVNNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPQSKPIPGNL
PFSFFPAGKTIKDVEQACAETPFPTLTTLPGPETSVQRIPPPPGA
3D structure
PDB1b80 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.
ChainB
Resolution1.73 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) H177 F194
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 D48 G66 D68 S70 D49 G67 D69 S71
BS02 CA B S177 D194 T196 I199 D201 S178 D195 T197 I200 D202
BS03 HEM B H39 I42 R43 F46 E146 P147 M172 L173 A175 H176 A179 A180 V181 D183 F193 H40 I43 R44 F47 E147 P148 M173 L174 A176 H177 A180 A181 V182 D184 F194
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:1b80, PDBe:1b80, PDBj:1b80
PDBsum1b80
PubMed11162097
UniProtP06181|LIG8_PHACH Ligninase H8 (Gene Name=LPOA)

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