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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4W7J

CRYSTAL STRUCTURE OF A DECOLORIZING PEROXIDASE (DYP) 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
C0004601molecular_functionperoxidase activity
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
C0098869biological_processcellular oxidant detoxification
C0140825molecular_functionlactoperoxidase activity
D0004601molecular_functionperoxidase activity
D0005576cellular_componentextracellular region
D0005829cellular_componentcytosol
D0016491molecular_functionoxidoreductase activity
D0020037molecular_functionheme binding
D0046872molecular_functionmetal ion binding
D0098869biological_processcellular oxidant detoxification
D0140825molecular_functionlactoperoxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues25
Detailsbinding site for residue HEM A 501
ChainResidue
AGLU162
AARG255
AHIS304
AILE305
ATHR308
AARG309
AARG311
AARG332
APHE359
APHE370
AILE398
APHE166
AVAL426
AHOH641
AHOH646
AHOH658
AHOH667
AHOH676
ALEU167
AASP168
AGLY169
AILE170
AALA171
AGLN221
AVAL253
site_idAC2
Number of Residues23
Detailsbinding site for residue HEM B 501
ChainResidue
BGLU162
BPHE166
BLEU167
BASP168
BGLY169
BILE170
BALA171
BGLN221
BARG255
BHIS304
BILE305
BTHR308
BARG309
BARG311
BARG332
BPHE359
BPHE370
BILE398
BHOH677
BHOH679
BHOH711
BHOH729
BHOH743
site_idAC3
Number of Residues24
Detailsbinding site for residue HEM C 501
ChainResidue
CGLU162
CPHE166
CLEU167
CASP168
CGLY169
CILE170
CALA171
CGLN221
CARG255
CHIS304
CILE305
CTHR308
CARG309
CARG311
CARG332
CPHE359
CPHE370
CGLN374
CILE398
CHOH669
CHOH674
CHOH685
CHOH705
CHOH753
site_idAC4
Number of Residues23
Detailsbinding site for residue HEM D 501
ChainResidue
DGLU162
DPHE166
DLEU167
DGLY169
DILE170
DALA171
DGLN221
DARG255
DHIS304
DILE305
DTHR308
DARG309
DARG311
DARG332
DPHE359
DPHE370
DGLN374
DILE398
DHOH673
DHOH676
DHOH679
DHOH695
DHOH697
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 Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23235158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"23235158","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25495127","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25542606","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2016","firstPage":"6277","lastPage":"6285","volume":"6","journal":"Catal. Sci. Technol.","title":"Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase.","authors":["Linde D.","Canellas M.","Davo-Siguero I.","Romero A.","Lucas F.","Ruiz-Duenas F.J.","Guallar V.","Martinez A.T."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/c6cy00539j"}]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2015","submissionDatabase":"PDB data bank","title":"Crystallographic Trapping of a Covalently Modified Heme in a Dye-Decolorizing Peroxidase.","authors":["Strittmatter E.","Piontek K.","Plattner D.A."]}},{"source":"PDB","id":"4AU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UZI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4W7J","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4W7K","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4W7L","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4W7M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4W7N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4W7O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AG0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IKD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5IKG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"23235158","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25542606","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2015","submissionDatabase":"PDB data bank","title":"Crystallographic Trapping of a Covalently Modified Heme in a Dye-Decolorizing Peroxidase.","authors":["Strittmatter E.","Piontek K.","Plattner D.A."]}},{"source":"PDB","id":"4AU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UZI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AG0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5AG1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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