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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 Residues1
DetailsACT_SITE: Nucleophile; for glutathione peroxidase activity => ECO:0000269|PubMed:10508415
ChainResidueDetails
ACYS680

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
ChainResidueDetails
ATYR36
ASER237
AHIS978
AHIS1022
AGLY45
ATYR48
AHIS101
ALYS109
AGLN124
AASP127
AASP128
AHIS161

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.29, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AHIS103
AHIS163
AHIS1020

site_idSWS_FT_FI4
Number of Residues9
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.29, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AHIS276
ACYS319
AHIS324
AHIS637
ACYS680
AHIS685
AMET690
AHIS1026
AMET1031

site_idSWS_FT_FI5
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17242517, ECO:0007744|PDB:2J5W
ChainResidueDetails
APHE389
AGLY398
ATYR401
ASER598
APHE748
AGLY757
ATYR760
ASER936

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.29, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AHIS975
ACYS1021

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:23843990, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AHIS980

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER703

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.29, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AASN119

site_idSWS_FT_FI10
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169
ChainResidueDetails
AASN339

site_idSWS_FT_FI11
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AASN378

site_idSWS_FT_FI12
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN569
AASN907

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|Ref.29, ECO:0007744|PDB:1KCW
ChainResidueDetails
AASN743

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a65
ChainResidueDetails
AHIS1020
AHIS1022
ACYS1021

223166

PDB entries from 2024-07-31

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