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3FM6

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 Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 350
ChainResidue
AHIS39
AALA172
AALA173
AALA174
AASP175
ALYS176
AVAL177
APHE186
ALEU228
ASER230
AGOL343
AGLU40
AHOH619
AHOH668
AHOH756
AHOH834
ALEU42
APHE46
AGLU140
APRO141
ALEU166
ASER168
AHIS169

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 351
ChainResidue
AASP48
AGLY60
AASP62
ASER64
AHOH493
AHOH505

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

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 332
ChainResidue
AASP30
AGLU37
AHIS232
AHOH368

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 333
ChainResidue
AGLU26
AASP237
AHOH390
AHOH608
AHOH623

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 334
ChainResidue
AHIS293
AASP318
AHOH448
AHOH454
AHOH455
AHOH677

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 335
ChainResidue
AHIS95
AHOH396
AHOH456
AHOH457
AHOH458

site_idAC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE ZN A 336
ChainResidue
AGLU36
AGLU40
AGLU83
AZN337
AFE338
AHOH461
AHOH519
AHOH675

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 337
ChainResidue
AGLU36
AGLU40
AGLU83
AZN336
AHOH459

site_idBC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FE A 338
ChainResidue
AGLU83
AASP175
AZN336
AHOH461
AHOH462
AHOH463
AHOH519
AHOH675
AHOH703

site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 339
ChainResidue
AASP69
ALYS89
AHOH666
AHOH700
AHOH776
AHOH877

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 340
ChainResidue
AFE341
AHOH465
AHOH555
AHOH679
AHOH721

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 341
ChainResidue
AASP128
AFE340
AHOH555
AHOH721
AHOH843

site_idBC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 342
ChainResidue
AHOH629
AHOH711
AHOH737
AHIS136
AVAL138
AASP143
AARG151
AHOH529
AHOH532
AHOH561

site_idBC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 343
ChainResidue
AARG43
APRO76
AALA77
AALA79
AGLU140
APRO141
ALYS176
AVAL177
AHEM350
AHOH534
AHOH866

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

227344

PDB entries from 2024-11-13

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