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5FNB

CRYSTAL STRUCTURE OF FUNGAL VERSATILE PEROXIDASE FROM PLEUROTUS ERYNGII SEPTUPLE MUTANT E37K, H39R, V160A, T184M, Q202L, D213A & G330R

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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP48
AGLY60
AASP62
ASER64
AHOH2069
AHOH2076

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AVAL192
AASP194
ASER170
AASP187
ATHR189

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 500
ChainResidue
AARG39
AGLU40
ALEU42
AARG43
APHE46
AGLU140
APRO141
ALEU165
ALEU166
ASER168
AHIS169
AALA172
AALA173
AALA174
AASP175
ALYS176
AVAL177
APHE186
ALEU228
ASER230
AHOH2058
AHOH2064
AHOH2065
AHOH2210
AHOH2214

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASP48
BGLY60
BASP62
BSER64
BHOH2049
BHOH2053

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BSER170
BASP187
BTHR189
BVAL192
BASP194

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE HEM B 500
ChainResidue
BARG39
BGLU40
BPHE46
BGLU140
BPRO141
BLEU166
BSER168
BHIS169
BALA172
BALA173
BALA174
BLEU228
BSER230
BMET262
BHOH2037
BHOH2039
BHOH2050

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 1330
ChainResidue
AARG257
AHOH2275
BASP143
BSER144
BSER147
BHOH2145
BHOH2152
BHOH2275
BHOH2276

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 1331
ChainResidue
BASP23
BPHE91
BLYS94
BHOH2277
BHOH2278

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

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. VResLRLtFHDA
ChainResidueDetails
AVAL38-ALA49

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
AHIS47
BHIS47

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Tryptophan radical intermediate => ECO:0000269|PubMed:16246366
ChainResidueDetails
ATRP164
BTRP164

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:16246366
ChainResidueDetails
AGLU36
AASP175
BGLU36
BASP175

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU40
BGLU40

site_idSWS_FT_FI5
Number of Residues20
DetailsBINDING:
ChainResidueDetails
AASP187
ATHR189
AVAL192
AASP194
BASP48
BGLY60
BASP62
BSER64
BSER170
BALA173
BASP187
BTHR189
BVAL192
BASP194
AASP62
ASER64
ASER170
AALA173
AASP48
AGLY60

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS169
BHIS169

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00297
ChainResidueDetails
AARG43
BARG43

site_idSWS_FT_FI8
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN96
BASN96

219869

PDB entries from 2024-05-15

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