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2W23

Structure of mutant W169Y of Pleurotus eryngii versatile peroxidase (VP)

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 A 1316
ChainResidue
AGLU36
ASER168
AHIS169
AALA172
AALA173
AALA174
AASP175
ALYS176
AVAL177
APHE186
ALEU228
AHIS39
ASER230
AHOH2046
AHOH2059
AHOH2358
AHOH2359
AHOH2360
AGLU40
ALEU42
APHE46
APRO139
AGLU140
APRO141
ALEU165

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1317
ChainResidue
AASP48
AGLY60
AASP62
ASER64
AHOH2065
AHOH2087

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 1318
ChainResidue
ASER170
AASP187
ATHR189
AVAL192
AASP194

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1319
ChainResidue
AHIS136
AGLU140
AARG206
AHOH2168
AHOH2176
AHOH2361
AHOH2362
AHOH2363

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 1320
ChainResidue
APRO115
ASER188
ATHR189
AVAL289
AGLY290
AHOH2364
AHOH2365
AHOH2366

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVYLLASHSI
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
ATYR164

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

225946

PDB entries from 2024-10-09

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