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3FM1

Crystal Structure Analysis of Fungal Versatile Peroxidase from Pleurotus eryngii

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 Residues27
DetailsBINDING SITE FOR RESIDUE HEM A 350
ChainResidue
AGLU36
ALEU166
ASER168
AHIS169
AALA172
AALA173
AALA174
AASP175
ALYS176
AVAL177
APHE186
AHIS39
ALEU228
ASER230
AMN353
AHOH434
AHOH470
AHOH805
AHOH1159
AHOH1160
AGLU40
ALEU42
AARG43
APHE46
AGLU140
APRO141
ALEU165

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 351
ChainResidue
AASP48
AGLY60
AASP62
ASER64
AHOH346
AHOH816

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 352
ChainResidue
ASER170
AASP187
ATHR189
AVAL192
AASP194

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A 353
ChainResidue
AGLU36
AGLU40
AASP175
AHEM350
AHOH1158
AHOH1159

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 332
ChainResidue
AASP30
AGLU37
AHIS232
AHOH420

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 333
ChainResidue
AGLU26
AASP237
ANA338
AHOH530
AHOH532
AHOH534
AHOH1174

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 334
ChainResidue
AHIS293
AASP318
AHOH1053
AHOH1129
AHOH1130
AHOH1133

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ZN A 335
ChainResidue
AGLU36
AGLU40
AGLU83
AFE336
AHOH432
AHOH755
AHOH1166
AHOH1167

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE FE A 336
ChainResidue
AGLU83
AASP175
AZN335
AHOH1163
AHOH1164
AHOH1165
AHOH1166
AHOH1167

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 337
ChainResidue
ANA340
AHOH508
AHOH512
AHOH513
AHOH1171
AHOH1175

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NA A 338
ChainResidue
AASP146
AZN333
AHOH528
AHOH529
AHOH530
AHOH532
AHOH864
AHOH1174

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 339
ChainResidue
AHOH940
AHOH941
AHOH942
AHOH943
AHOH944
AHOH945

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 340
ChainResidue
AHOH505
AHOH506
AHOH508
AHOH513
AHOH1171
AASP128
AFE337

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 341
ChainResidue
APHE142
AHOH522
AHOH523
AHOH524
AHOH525
AHOH1170

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 342
ChainResidue
AHOH1177
AHOH1178
AHOH1181
AHOH1183
AHOH1184
AHOH1185

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. VHesLRLtFHDA
ChainResidueDetails
AVAL38-ALA49

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
AHIS47

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Tryptophan radical intermediate => ECO:0000269|PubMed:16246366
ChainResidueDetails
ATRP164

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16246366
ChainResidueDetails
AGLU36
AASP175

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AGLU40

site_idSWS_FT_FI5
Number of Residues10
DetailsBINDING:
ChainResidueDetails
AASP48
AASP194
AGLY60
AASP62
ASER64
ASER170
AALA173
AASP187
ATHR189
AVAL192

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS169

site_idSWS_FT_FI7
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000255|PROSITE-ProRule:PRU00297
ChainResidueDetails
AARG43

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN96

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AHIS47
AARG43
AASN78

225158

PDB entries from 2024-09-18

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