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5FW4

Structure of Thermobifida fusca DyP-type Peroxidase and Activity towards Kraft Lignin and Lignin Model Compounds

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0020037molecular_functionheme binding
B0004601molecular_functionperoxidase activity
B0020037molecular_functionheme binding
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM A 401
ChainResidue
AASN197
APRO305
AARG315
ALEU334
APHE336
APHE347
AGLN351
ALEU361
AILE365
AOXY402
AHOH2170
AGLN201
AHOH2171
AILE202
AGLY204
ATHR205
AALA206
AILE243
AHIS299
AALA303

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY A 402
ChainResidue
AASP203
AARG315
APHE336
AHEM401

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM B 401
ChainResidue
BASN197
BGLN201
BILE202
BGLY204
BTHR205
BALA206
BILE243
BMET245
BHIS299
BALA303
BPRO305
BARG315
BPHE336
BPHE347
BGLN351
BLEU361
BOXY402
BHOH2168

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OXY B 402
ChainResidue
BASP203
BARG315
BPHE336
BHEM401

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsCompositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"19967355","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"proximal binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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