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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
A0016491molecular_functionoxidoreductase activity
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
B0016491molecular_functionoxidoreductase activity
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
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8000874","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AHIS47
AASN84
AARG43

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
BHIS47
BASN84
BARG43

247536

PDB entries from 2026-01-14

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