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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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:19967355
ChainResidueDetails
AASP203
BASP203

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: proximal binding residue => ECO:0000305
ChainResidueDetails
AHIS299
BHIS299

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PDB entries from 2024-07-10

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