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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
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_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
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS47
BHIS47

site_idSWS_FT_FI2
Number of Residues18
DetailsBINDING:
ChainResidueDetails
AASP48
BASP48
BGLY66
BASP68
BSER70
BSER177
BASP194
BTHR196
BILE199
BASP201
AGLY66
AASP68
ASER70
ASER177
AASP194
ATHR196
AILE199
AASP201

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
DetailsMOD_RES: 3-hydroxytryptophan => ECO:0000269|PubMed:10024453
ChainResidueDetails
ATRP171
BTRP171

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN257
BASN257

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

226707

PDB entries from 2024-10-30

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