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1QPA

LIGNIN PEROXIDASE ISOZYME LIP4.65 (PI 4.65)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0016690molecular_functiondiarylpropane peroxidase activity
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0046274biological_processlignin catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
B0000302biological_processresponse to reactive oxygen species
B0004601molecular_functionperoxidase activity
B0006979biological_processresponse to oxidative stress
B0016690molecular_functiondiarylpropane peroxidase activity
B0020037molecular_functionheme binding
B0034599biological_processcellular response to oxidative stress
B0042744biological_processhydrogen peroxide catabolic process
B0046274biological_processlignin catabolic process
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idHE3
Number of Residues2
DetailsHEM 350
ChainResidue
AHEM350
BHEM350

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. ETVWLLSAHSI
ChainResidueDetails
AGLU168-ILE178

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. AHeaLRMvFHDS
ChainResidueDetails
AALA38-SER49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS47
BHIS47

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AASP48
ATHR196
AGLN199
AASP201
BASP48
BGLY66
BASP68
BSER70
BSER177
BASP194
BTHR196
BGLN199
BASP201
AGLY66
AASP68
ASER70
ASER177
AASP194

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS176
BHIS176

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG43
BARG43

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8000874
ChainResidueDetails
AASN257
BASN257

221051

PDB entries from 2024-06-12

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