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3FMU

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 Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 350
ChainResidue
AHIS39
AHIS169
AALA172
AALA173
AALA174
AASP175
ALYS176
AVAL177
APHE186
ALEU228
ASER230
AGLU40
AZN337
AHOH455
AHOH457
AHOH678
AHOH720
ALEU42
APHE46
AGLU140
APRO141
ALEU165
ALEU166
ASER168

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 351
ChainResidue
AASP48
AGLY60
AASP62
ASER64
AHOH395
AHOH472

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
AHOH403

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 333
ChainResidue
AGLU26
AASP237
AHOH408
AHOH617
AHOH682

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 334
ChainResidue
AASP143
ACAC345
AHOH638

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 335
ChainResidue
AHIS293
AASP318
AHOH486
AHOH487
AHOH488
AHOH728

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 336
ChainResidue
AHIS95
AHOH465
AHOH855

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 337
ChainResidue
AGLU40
AASP175
AHEM350

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 338
ChainResidue
AHIS136
ACAC345
AHOH625
AHOH626

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 339
ChainResidue
AGLU36
AGLU40
AGLU83
AZN340
AHOH608

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 340
ChainResidue
AGLU36
AGLU40
AGLU83
AZN339
AHOH664

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 341
ChainResidue
AGLU83
AASP175
AHOH456
AHOH607
AHOH608
AHOH609

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 342
ChainResidue
AASP69
ALYS89
AHOH630
AHOH631
AHOH746

site_idBC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE A 343
ChainResidue
AFE344
AHOH466
AHOH632

site_idBC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 344
ChainResidue
AASP128
AFE343
AHOH632
AHOH858

site_idBC8
Number of Residues13
DetailsBINDING SITE FOR RESIDUE CAC A 345
ChainResidue
AHOH627
AHOH638
AHOH660
AHOH776
AHOH861
AHIS136
AVAL138
AASP143
AZN334
AZN338
AHOH370
AHOH567
AHOH625

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVSLLASHSI
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
ASER164

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

226707

PDB entries from 2024-10-30

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