Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1KCW

X-RAY CRYSTAL STRUCTURE OF HUMAN CERULOPLASMIN AT 3.0 ANGSTROMS

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004322	molecular_function	ferroxidase activity
A	0004602	molecular_function	glutathione peroxidase activity
A	0005507	molecular_function	copper ion binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005765	cellular_component	lysosomal membrane
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005886	cellular_component	plasma membrane
A	0006878	biological_process	intracellular copper ion homeostasis
A	0006879	biological_process	intracellular iron ion homeostasis
A	0016491	molecular_function	oxidoreductase activity
A	0016722	molecular_function	oxidoreductase activity, acting on metal ions
A	0016724	molecular_function	oxidoreductase activity, acting on metal ions, oxygen as acceptor
A	0036479	molecular_function	peroxidase inhibitor activity
A	0046872	molecular_function	metal ion binding
A	0047066	molecular_function	phospholipid-hydroperoxide glutathione peroxidase activity
A	0051087	molecular_function	protein-folding chaperone binding
A	0070062	cellular_component	extracellular exosome
A	0072562	cellular_component	blood microparticle
A	0098869	biological_process	cellular oxidant detoxification

Functional Information from PDB Data

site_id	CU1
Number of Residues	5
Details	TYPE I CU BINDING SITE IN DOMAIN 2. AT BEST LEU 329 MAY HAVE VAN DER WAALS CONTACT WITH THE CU.

Chain	Residue
A	CU1049
A	HIS276
A	CYS319
A	HIS324
A	LEU329

site_id	CU2
Number of Residues	5
Details	TYPE I CU BINDING SITE IN DOMAIN 4.

Chain	Residue
A	MET690
A	CU1053
A	HIS637
A	CYS680
A	HIS685

site_id	CU3
Number of Residues	5
Details	LABILE CU BINDING SITE IN DOMAIN 4.

Chain	Residue
A	CU1054
A	GLU597
A	HIS602
A	ASP684
A	GLU971

site_id	CU4
Number of Residues	5
Details	TYPE I CU BINDING SITE IN DOMAIN 6.

Chain	Residue
A	CU1055
A	HIS975
A	CYS1021
A	HIS1026
A	MET1031

site_id	CU5
Number of Residues	5
Details	LABILE CU BINDING SITE IN DOMAIN 6.

Chain	Residue
A	CU1056
A	GLU272
A	GLU935
A	HIS940
A	ASP1025

site_id	TRI
Number of Residues	13
Details	TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34.

Chain	Residue
A	CU1050
A	CU1051
A	O1057
A	CU1052
A	O1058
A	HIS101
A	HIS103
A	HIS161
A	HIS163
A	HIS978
A	HIS980
A	HIS1020
A	HIS1022

Functional Information from PROSITE/UniProt

site_id	PS00079
Number of Residues	21
Details	MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF

Chain	Residue	Details
A	GLY313-PHE333
A	GLY674-TYR694
A	GLY1015-TYR1035

site_id	PS00080
Number of Residues	12
Details	MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM

Chain	Residue	Details
A	HIS1020-MET1031

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	180
Details	Domain: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	148
Details	Domain: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	148
Details	Domain: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	170
Details	Domain: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"description":"Nucleophile; for glutathione peroxidase activity","evidences":[{"source":"PubMed","id":"10508415","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	12
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	9
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17242517","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2J5W","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Binding 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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23843990","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ENZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Glycosylation: {"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"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1a65

Chain	Residue	Details
A	HIS1020
A	HIS1022
A	CYS1021

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)