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4BM0

CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE I FROM PLEUROTUS OSTREATUS - CRYSTAL FORM VII

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 401
ChainResidue
AASP49
AGLY52
AGLY61
AASP63
ASER65
ASER134

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AVAL193
AASP195
ASER171
AASP188
ATHR190

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AHIS40
AGLU41
ALEU43
AARG44
APHE47
APRO140
AGLU141
APRO142
ALEU167
ASER169
AHIS170
AALA173
AALA174
AALA175
AASP176
ALYS177
AVAL178
APHE187
ALEU229
ASER231
AHOH2012
AHOH2013

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 2024-09-11

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