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2VKA

Site-Directed Mutagenesis of the Catalytic Tryptophan Environment in Pleurotus eryngii Versatile Peroxidase

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 Residues25
DetailsBINDING SITE FOR RESIDUE HEM A1320
ChainResidue
AGLU36
ALEU166
ASER168
AHIS169
AALA172
AALA173
AASP175
ALYS176
AVAL177
APHE186
ALEU228
AHIS39
ASER230
AHOH2058
AHOH2071
AHOH2415
AHOH2416
AHOH2417
AGLU40
ALEU42
ATHR45
APHE46
AGLU140
APRO141
ALEU165

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A1318
ChainResidue
AHIS136
AGLU140
AARG206
AHOH2207
AHOH2213
AHOH2411
AHOH2412
AHOH2413
AHOH2414

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A1319
ChainResidue
ASER170
AASP187
ATHR189
AVAL192
AASP194

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A1321
ChainResidue
AASP48
AGLY60
AASP62
ASER64
AHOH2074
AHOH2103

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A1322
ChainResidue
ASER53
ATHR55
AARG151
AASP154
AGLY297
AHOH2231
AHOH2418

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
ASER64
ASER170
AALA173
AASP187
ATHR189
AVAL192
AASP194
AGLY60
AASP62

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

219869

PDB entries from 2024-05-15

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