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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2J5W

Ceruloplasmin revisited: structural and functional roles of various metal cation binding sites

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
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
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
Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
AHIS1020
AHIS1022
ACYS1021

238895

PDB entries from 2025-07-16

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