Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4ENZ

Structure of human ceruloplasmin at 2.6 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0005507molecular_functioncopper ion binding
A0016491molecular_functionoxidoreductase activity
Functional Information from PROSITE/UniProt
site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM
ChainResidueDetails
AHIS1020-MET1031

site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF
ChainResidueDetails
AGLY313-PHE333
AGLY674-TYR694
AGLY1015-TYR1035

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4ENZ
ChainResidueDetails
ATYR36
AGLY45
ATYR48
ALYS109
AGLN124
AASP127
AASP128
ASER237

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: type 2 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AHIS101
AHIS978

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: type 3 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AHIS103
AHIS161
AHIS163
AHIS980
AHIS1020
AHIS1022

site_idSWS_FT_FI4
Number of Residues9
DetailsBINDING: type 1 copper site => ECO:0000269|PubMed:17242517, ECO:0000269|PubMed:23843990, ECO:0000269|Ref.27, 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.27, 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
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
ASER703

site_idSWS_FT_FI8
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.27, ECO:0007744|PDB:1KCW, ECO:0007744|PDB:2J5W, ECO:0007744|PDB:4EJX, ECO:0007744|PDB:4ENZ
ChainResidueDetails
AASN119

site_idSWS_FT_FI9
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_FI10
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_FI11
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
AASN569
AASN907

site_idSWS_FT_FI12
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.27, ECO:0007744|PDB:1KCW
ChainResidueDetails
AASN743

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon