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5IKD

Asymmetric sulfoxidation by engineering the heme pocket of a dye-decolorizing peroxidase

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
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue HEM A 501
ChainResidue
AGLU162
AILE305
ATHR308
AARG309
AARG311
AARG332
APHE370
AILE398
AHOH610
AHOH697
AHOH701
APHE166
AHOH730
AHOH918
ALEU167
AGLY169
AILE170
AALA171
AGLN221
AARG255
AHIS304

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 Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23235158","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
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 Residues3
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 Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

244693

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