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4BLZ

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

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
B0000302biological_processresponse to reactive oxygen species
B0004601molecular_functionperoxidase activity
B0005576cellular_componentextracellular region
B0006979biological_processresponse to oxidative stress
B0016689molecular_functionmanganese peroxidase activity
B0020037molecular_functionheme binding
B0034599biological_processcellular response to oxidative stress
B0042744biological_processhydrogen peroxide catabolic process
B0046274biological_processlignin catabolic process
B0046872molecular_functionmetal ion binding
B0052750molecular_functionreactive-black-5:hydrogen-peroxide oxidoreductase activity
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
ASER171
AASP188
ATHR190
AVAL193
AASP195

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AHOH2064
AHOH2072
AASP49
AGLY61
AASP63
ASER65

site_idAC3
Number of Residues26
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
AHOH2049
AHOH2052
AHOH2057
AHOH2058
AHOH2059
AHOH2066
AHOH2211

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 400
ChainResidue
BSER171
BASP188
BTHR190
BVAL193
BASP195

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASP49
BGLY61
BASP63
BSER65
BHOH2061
BHOH2066

site_idAC6
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BHIS40
BGLU41
BLEU43
BARG44
BPHE47
BGLU141
BPRO142
BLEU167
BSER169
BHIS170
BALA173
BALA174
BALA175
BASP176
BLYS177
BVAL178
BPHE187
BLEU229
BSER231
BHOH2052
BHOH2057
BHOH2058
BHOH2062
BHOH2218

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000255|PROSITE-ProRule:PRU10012
ChainResidueDetails
AHIS48
BHIS48

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Tryptophan radical intermediate => ECO:0000250
ChainResidueDetails
ATRP165
BTRP165

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU37
AGLU41
AALA174
AASP176
BGLU37
BGLU41
BALA174
BASP176

site_idSWS_FT_FI4
Number of Residues18
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00297
ChainResidueDetails
AASP49
BASP49
BGLY61
BASP63
BSER65
BSER171
BASP188
BTHR190
BVAL193
BASP195
AGLY61
AASP63
ASER65
ASER171
AASP188
ATHR190
AVAL193
AASP195

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00297
ChainResidueDetails
AHIS170
BHIS170

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00297
ChainResidueDetails
AARG44
BARG44

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN97
BASN97

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PDB entries from 2024-11-13

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