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6A6Q

Crystal structure of a lignin peroxidase isozyme H8 variant that is stable at very acidic pH

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0016491molecular_functionoxidoreductase activity
A0016690molecular_functiondiarylpropane peroxidase activity
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0046274biological_processlignin catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue HEB A 401
ChainResidue
AHIS39
AMET172
ALEU173
AALA175
AHIS176
AALA179
AALA180
AVAL181
AASN182
AASP183
APHE193
AGLU40
ASER237
AHOH511
AHOH553
AHOH581
AHOH618
AHOH653
AILE42
AARG43
APHE46
AILE85
APRO145
AGLU146
APRO147

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AASP48
AGLY66
AASP68
ASER70
AHOH526
AHOH595

site_idAC3
Number of Residues5
Detailsbinding site for residue CA A 403
ChainResidue
ASER177
AASP194
ATHR196
AILE199
AASP201

site_idAC4
Number of Residues6
Detailsbinding site for residue GOL A 404
ChainResidue
ASER13
ATRP17
AVAL103
ATHR104
AASP107
AHOH541

site_idAC5
Number of Residues6
Detailsbinding site for residue GOL A 405
ChainResidue
ASER4
AASN5
ACYS15
AALA16
APHE18
AASP19

site_idAC6
Number of Residues5
Detailsbinding site for residue GOL A 406
ChainResidue
AGLU57
APHE62
AGLY64
AGLY65
AHOH506

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. ELVWMLSAHSV
ChainResidueDetails
AGLU168-VAL178

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. AHesIRLvFHDS
ChainResidueDetails
AALA38-SER49

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues11
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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