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4AU9

Crystal Structure of a Fungal DyP-Type Peroxidase from Auricularia auricula-judae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
A0140825molecular_functionlactoperoxidase activity
B0004601molecular_functionperoxidase activity
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
B0140825molecular_functionlactoperoxidase activity
Functional Information from PROSITE/UniProt
site_idPS00059
Number of Residues15
DetailsADH_ZINC Zinc-containing alcohol dehydrogenases signature. GHEmFGFldgiAqpA
ChainResidueDetails
AGLY160-ALA174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:23235158
ChainResidueDetails
AASP168
BASP168

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25495127, ECO:0000269|PubMed:25542606, ECO:0000269|DOI:10.1039/c6cy00539j, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:4W7J, ECO:0007744|PDB:4W7K, ECO:0007744|PDB:4W7L, ECO:0007744|PDB:4W7M, ECO:0007744|PDB:4W7N, ECO:0007744|PDB:4W7O, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5IKD, ECO:0007744|PDB:5IKG
ChainResidueDetails
AHIS304
BHIS304

site_idSWS_FT_FI3
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23235158, ECO:0000269|PubMed:25542606, ECO:0000269|Ref.8, ECO:0007744|PDB:4AU9, ECO:0007744|PDB:4UZI, ECO:0007744|PDB:5AG0, ECO:0007744|PDB:5AG1
ChainResidueDetails
AASN282
AASN349
AASN415
BASN282
BASN349
BASN415

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN322
BASN322

217705

PDB entries from 2024-03-27

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