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4BLK

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0006979biological_processresponse to oxidative stress
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
AHOH2094
AHOH2102

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

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AHIS40
AGLU41
ALEU43
AARG44
APHE47
AGLU141
APRO142
ALEU166
ALEU167
ASER169
AHIS170
AALA173
AALA174
AALA175
AASP176
ALYS177
AVAL178
APHE187
ALEU229
ASER231
AHOH2075
AHOH2077
AHOH2078
AHOH2088
AHOH2282

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012
ChainResidueDetails
AHIS48

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Tryptophan radical intermediate => ECO:0000250
ChainResidueDetails
ATRP165

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU37
AGLU41
AALA174
AASP176

site_idSWS_FT_FI4
Number of Residues9
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00297
ChainResidueDetails
AASP49
AGLY61
AASP63
ASER65
ASER171
AASP188
ATHR190
AVAL193
AASP195

site_idSWS_FT_FI5
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00297
ChainResidueDetails
AHIS170

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00297
ChainResidueDetails
AARG44

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN97

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PDB entries from 2024-07-10

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