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1LLP

LIGNIN PEROXIDASE (ISOZYME H2) PI 4.15

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
Functional Information from PDB Data
site_idHE3
Number of Residues1
Details
ChainResidue
AHEM350

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 Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS47

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING:
ChainResidueDetails
AASP48
AGLY66
AASP68
ASER70
ASER177
AASP194
ATHR196
AILE199
AASP201

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS176

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG43

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: 3-hydroxytryptophan => ECO:0000269|PubMed:10024453
ChainResidueDetails
ATRP171

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN257

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

226707

PDB entries from 2024-10-30

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