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2BOQ

Crystal structure of 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
A0016491molecular_functionoxidoreductase activity
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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1323
ChainResidue
AASP30
AGLU37
AHIS232
AARG236
AHOH2376

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1324
ChainResidue
AGLU26
AASP237
AHOH2377
AHOH2378

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1325
ChainResidue
AHIS136
AGLU140
AZN1326
ACAC1329

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A1326
ChainResidue
AGLU140
AZN1325
AZN1327

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1327
ChainResidue
AGLU140
AASP143
AZN1326
ACAC1329

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MN A1328
ChainResidue
AGLU36
AASP175
AHEM1320

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CAC A1329
ChainResidue
AHIS136
AVAL138
AGLU140
AASP143
AZN1325
AZN1327
AHOH2195

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A1351
ChainResidue
AASP48
AGLY60
AASP62
ASER64
AHOH2081
AHOH2110

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A1352
ChainResidue
ASER170
AASP187
ATHR189
AVAL192
AASP194

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1358
ChainResidue
AHIS293
AASP318
AHOH2379
AHOH2380

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A1359
ChainResidue
AHIS95
AHOH2024
AHOH2381

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1360
ChainResidue
AHOH2177
AHOH2382
AHOH2383
AHOH2384

site_idBC4
Number of Residues27
DetailsBINDING SITE FOR RESIDUE HEM A1320
ChainResidue
AGLU36
AHIS39
AGLU40
ALEU42
AARG43
APHE46
APRO139
AGLU140
APRO141
ALEU165
ALEU166
ASER168
AHIS169
AALA172
AALA173
AALA174
AASP175
ALYS176
AVAL177
APHE186
ALEU228
ASER230
AMN1328
AHOH2060
AHOH2073
AHOH2374
AHOH2375

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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10012","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16246366","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues13
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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

246704

PDB entries from 2025-12-24

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