Structure of PDB 6a6q Chain A

Receptor sequence
>6a6qA (length=345) Species: 273507 (Phanerochaete chrysosporium RP-78) [Search protein sequence]
KRATCSNGKTVGDASCCAWFDVLDDIQQNLFHGGQCGAEAHESIRLVFHD
SIAISPRMEAQGKFGGGGADGSIMIFDDIETAFHPNIGLDEIVKLQKPFV
QKHGVTPGDFIAFAGRVALSNCPGAPQMNFFTGRAPATQPAPDGLVPEPF
HTVDQIIERVNDAGEFDELELVWMLSAHSVAAVNDVDPTVQGLPFDSTPG
IFDSQFFVETQLRGTAFPGSGGNQGEVESPLPGEIRIQSDETIARDSRTA
CEWQSFVNNQSKLVDDFQFIFLALTQLGQDPNAMTDCSDVIPQSKPIPGN
LPFSFFPAGKTIKDVEQACAETPFPTLTTLPGPETSVQRIPPPPG
3D structure
PDB6a6q In silico-designed lignin peroxidase fromPhanerochaete chrysosporiumshows enhanced acid stability for depolymerization of lignin.
ChainA
Resolution1.67 Å
3D
structure
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Enzymatic activity
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 HEB A H39 I42 R43 F46 E146 P147 M172 L173 A175 H176 A179 A180 V181 D183 F193 H41 I44 R45 F48 E148 P149 M174 L175 A177 H178 A181 A182 V183 D185 F195
BS02 CA A D48 G66 D68 S70 D50 G68 D70 S72
BS03 CA A S177 D194 T196 I199 D201 S179 D196 T198 I201 D203
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
View graph for
Biological Process
External links
PDB RCSB:6a6q, PDBe:6a6q, PDBj:6a6q
PDBsum6a6q
PubMed30555531
UniProtP06181|LIG8_PHACH Ligninase H8 (Gene Name=LPOA)

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