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1SCH

PEANUT PEROXIDASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
A0140825molecular_functionlactoperoxidase activity
B0004601molecular_functionperoxidase activity
B0005576cellular_componentextracellular region
B0006979biological_processresponse to oxidative stress
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
B0140825molecular_functionlactoperoxidase activity
Functional Information from PDB Data
site_idADC
Number of Residues6
DetailsDISTAL CATION SITE THROUGH SOLVENT.
ChainResidue
ASER52
AGLU64
AASP43
AVAL46
AGLY48
AASP50

site_idADH
Number of Residues4
DetailsDISTAL HEME POCKET.
ChainResidue
AHIS42
AARG38
APHE41
AASN70

site_idAPC
Number of Residues5
DetailsPROXIMAL CATION SITE.
ChainResidue
ATHR170
AASP214
ATHR217
ALYS220
AASP222

site_idAPH
Number of Residues3
DetailsPROXIMAL HEME POCKET.
ChainResidue
AHIS169
APHE213
AASP239

site_idBDC
Number of Residues6
DetailsDISTAL CATION SITE THROUGH SOLVENT.
ChainResidue
BASP43
BVAL46
BGLY48
BASP50
BSER52
BGLU64

site_idBDH
Number of Residues4
DetailsDISTAL HEME POCKET.
ChainResidue
BHIS42
BARG38
BPHE41
BASN70

site_idBPC
Number of Residues5
DetailsPROXIMAL CATION SITE.
ChainResidue
BTHR170
BASP214
BTHR217
BLYS220
BASP222

site_idBPH
Number of Residues3
DetailsPROXIMAL HEME POCKET.
ChainResidue
BHIS169
BPHE213
BASP239

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. ELVTLSGAHTI
ChainResidueDetails
AGLU161-ILE171

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GAslLRLhFHDC
ChainResidueDetails
AGLY33-CYS44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
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"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000185"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AARG38
AHIS42
AASN70

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
BARG38
BHIS42
BASN70

246704

PDB entries from 2025-12-24

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