Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4EJX

Structure of ceruloplasmin-myeloperoxidase complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
B0004601molecular_functionperoxidase activity
B0006979biological_processresponse to oxidative stress
B0020037molecular_functionheme binding
D0004601molecular_functionperoxidase activity
D0006979biological_processresponse to oxidative stress
D0020037molecular_functionheme binding
Functional Information from PROSITE/UniProt
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF
ChainResidueDetails
AGLY313-PHE333
AGLY674-TYR694
AGLY1015-TYR1035
site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM
ChainResidueDetails
AHIS1020-MET1031
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EMPELTSMHTL
ChainResidueDetails
DGLU242-LEU252
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues180
DetailsDomain: {"description":"Plastocyanin-like 1","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1996","firstPage":"15","lastPage":"23","volume":"1","journal":"J. Biol. Inorg. Chem.","title":"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres.","authors":["Zaitseva I.","Zaitsev V.","Card G.","Moshkov K.","Bax B.","Ralph A.","Lindley P."]}},{"source":"PDB","id":"1KCW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues148
DetailsDomain: {"description":"Plastocyanin-like 2","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1996","firstPage":"15","lastPage":"23","volume":"1","journal":"J. Biol. Inorg. Chem.","title":"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres.","authors":["Zaitseva I.","Zaitsev V.","Card G.","Moshkov K.","Bax B.","Ralph A.","Lindley P."]}},{"source":"PDB","id":"1KCW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues148
DetailsDomain: {"description":"Plastocyanin-like 4","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1996","firstPage":"15","lastPage":"23","volume":"1","journal":"J. Biol. Inorg. Chem.","title":"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres.","authors":["Zaitseva I.","Zaitsev V.","Card G.","Moshkov K.","Bax B.","Ralph A.","Lindley P."]}},{"source":"PDB","id":"1KCW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues170
DetailsDomain: {"description":"Plastocyanin-like 5","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1996","firstPage":"15","lastPage":"23","volume":"1","journal":"J. Biol. Inorg. Chem.","title":"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres.","authors":["Zaitseva I.","Zaitsev V.","Card G.","Moshkov K.","Bax B.","Ralph A.","Lindley P."]}},{"source":"PDB","id":"1KCW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Nucleophile; for glutathione peroxidase activity","evidences":[{"source":"PubMed","id":"10508415","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17242517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J5W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues3
DetailsBinding site: {"description":"type 3 copper site","evidences":[{"source":"PubMed","id":"17242517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1996","firstPage":"15","lastPage":"23","volume":"1","journal":"J. Biol. Inorg. Chem.","title":"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres.","authors":["Zaitseva I.","Zaitsev V.","Card G.","Moshkov K.","Bax B.","Ralph A.","Lindley P."]}},{"source":"PDB","id":"1KCW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J5W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues9
DetailsBinding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"17242517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1996","firstPage":"15","lastPage":"23","volume":"1","journal":"J. Biol. Inorg. Chem.","title":"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres.","authors":["Zaitseva I.","Zaitsev V.","Card G.","Moshkov K.","Bax B.","Ralph A.","Lindley P."]}},{"source":"PDB","id":"1KCW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J5W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17242517","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J5W","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsBinding site: {"description":"type 1 copper site","evidences":[{"source":"PubMed","id":"17242517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1996","firstPage":"15","lastPage":"23","volume":"1","journal":"J. Biol. Inorg. Chem.","title":"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres.","authors":["Zaitseva I.","Zaitsev V.","Card G.","Moshkov K.","Bax B.","Ralph A.","Lindley P."]}},{"source":"PDB","id":"1KCW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J5W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ENZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17242517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1996","firstPage":"15","lastPage":"23","volume":"1","journal":"J. Biol. Inorg. Chem.","title":"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres.","authors":["Zaitseva I.","Zaitsev V.","Card G.","Moshkov K.","Bax B.","Ralph A.","Lindley P."]}},{"source":"PDB","id":"1KCW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2J5W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17242517","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J5W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1996","firstPage":"15","lastPage":"23","volume":"1","journal":"J. Biol. Inorg. Chem.","title":"The X-ray structure of human serum ceruloplasmin at 3.1 A: nature of the copper centres.","authors":["Zaitseva I.","Zaitsev V.","Card G.","Moshkov K.","Bax B.","Ralph A.","Lindley P."]}},{"source":"PDB","id":"1KCW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues3
DetailsBinding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10766826","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11705390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D2V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1D7W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DNU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DNW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MHL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CXP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"7840679","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000220","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16740002","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4EJX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20332087","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 601
ChainResidueDetails
BHIS95proton shuttle (general acid/base)

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon