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4BLL

Crystal Structure of Fungal Versatile Peroxidase I from Pleurotus ostreatus - Crystal Form II

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0016689molecular_functionmanganese peroxidase activity
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0046274biological_processlignin catabolic process
A0046872molecular_functionmetal ion binding
A0052750molecular_functionreactive-black-5:hydrogen-peroxide oxidoreductase activity
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AASP49
AGLY61
AASP63
ASER65
AHOH2086
AHOH2094

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AVAL193
AASP195
ASER171
AASP188
ATHR190

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AHIS40
AGLU41
ALEU43
AARG44
APHE47
APRO140
AGLU141
APRO142
ALEU166
ALEU167
ASER169
AHIS170
AALA173
AALA174
AALA175
AASP176
ALYS177
AVAL178
APHE187
ALEU229
ASER231
AHOH2071
AHOH2072
AHOH2076
AHOH2077
AHOH2251

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1320
ChainResidue
AGLU27
AASP238
AHOH2226
AHOH2320

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1321
ChainResidue
AASP31
AGLU38
AHIS233
AHOH2047

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 1322
ChainResidue
AGLU37
AGLU41
AGLU84
AHOH2064
AHOH2065

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVWLLASHSI
ChainResidueDetails
AGLU162-ILE172

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. VHesLRLtFHDA
ChainResidueDetails
AVAL39-ALA50

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10012","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Tryptophan radical intermediate","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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