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1LGA

CRYSTALLOGRAPHIC REFINEMENT OF LIGNIN PEROXIDASE AT 2 ANGSTROMS

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_idHPA
Number of Residues1
DetailsRESIDUE IN CHAIN A THAT H-BONDS WITH PROXIMAL HIS 176
ChainResidue
AASP238

site_idHPB
Number of Residues1
DetailsRESIDUE IN CHAIN B THAT H-BONDS WITH PROXIMAL HIS 176
ChainResidue
BASP238

site_idPBA
Number of Residues3
DetailsDISTAL RESIDUES IN CHAIN A FORMING THE PEROXIDE BINDING POCKET. THIS IS ANALOGOUS TO THE ARG-TRP-HIS FOUND IN CYTOCHROME C PEROXIDASE
ChainResidue
AARG43
APHE46
AHIS47

site_idPBB
Number of Residues3
DetailsDISTAL RESIDUES IN CHAIN B FORMING THE PEROXIDE BINDING POCKET. THIS IS ANALOGOUS TO THE ARG-TRP-HIS FOUND IN CYTOCHROME C PEROXIDASE
ChainResidue
BARG43
BPHE46
BHIS47

site_idPHA
Number of Residues1
DetailsRESIDUES BOUND TO PROXIMAL HEME LIGAND, CHAIN A
ChainResidue
AHIS176

site_idPHB
Number of Residues1
DetailsRESIDUES BOUND TO PROXIMAL HEME LIGAND, CHAIN B
ChainResidue
BHIS176

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. ELVWMLSAHSV
ChainResidueDetails
AGLU168-VAL178

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. AHesIRLvFHDS
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
DetailsModified residue: {"description":"3-hydroxytryptophan","evidences":[{"source":"PubMed","id":"10024453","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
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

250059

PDB entries from 2026-03-04

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