Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5N4L

Rat ceruloplasmin trigonal form

Functional Information from GO Data
ChainGOidnamespacecontents
A0001889biological_processliver development
A0004322molecular_functionferroxidase activity
A0004602molecular_functionglutathione peroxidase activity
A0005507molecular_functioncopper ion binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0006878biological_processintracellular copper ion homeostasis
A0006879biological_processintracellular iron ion homeostasis
A0006954biological_processinflammatory response
A0007005biological_processmitochondrion organization
A0007565biological_processfemale pregnancy
A0007584biological_processresponse to nutrient
A0007595biological_processlactation
A0009986cellular_componentcell surface
A0010467biological_processgene expression
A0015679biological_processplasma membrane copper ion transport
A0016042biological_processlipid catabolic process
A0016491molecular_functionoxidoreductase activity
A0016724molecular_functionoxidoreductase activity, acting on metal ions, oxygen as acceptor
A0019395biological_processfatty acid oxidation
A0030324biological_processlung development
A0032868biological_processresponse to insulin
A0042593biological_processglucose homeostasis
A0046688biological_processresponse to copper ion
A0046872molecular_functionmetal ion binding
A0047066molecular_functionphospholipid-hydroperoxide glutathione peroxidase activity
A0051087molecular_functionprotein-folding chaperone binding
A0060056biological_processmammary gland involution
A0061762biological_processCAMKK-AMPK signaling cascade
A0065003biological_processprotein-containing complex assembly
A0098869biological_processcellular oxidant detoxification
B0001889biological_processliver development
B0004322molecular_functionferroxidase activity
B0004602molecular_functionglutathione peroxidase activity
B0005507molecular_functioncopper ion binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0006878biological_processintracellular copper ion homeostasis
B0006879biological_processintracellular iron ion homeostasis
B0006954biological_processinflammatory response
B0007005biological_processmitochondrion organization
B0007565biological_processfemale pregnancy
B0007584biological_processresponse to nutrient
B0007595biological_processlactation
B0009986cellular_componentcell surface
B0010467biological_processgene expression
B0015679biological_processplasma membrane copper ion transport
B0016042biological_processlipid catabolic process
B0016491molecular_functionoxidoreductase activity
B0016724molecular_functionoxidoreductase activity, acting on metal ions, oxygen as acceptor
B0019395biological_processfatty acid oxidation
B0030324biological_processlung development
B0032868biological_processresponse to insulin
B0042593biological_processglucose homeostasis
B0046688biological_processresponse to copper ion
B0046872molecular_functionmetal ion binding
B0047066molecular_functionphospholipid-hydroperoxide glutathione peroxidase activity
B0051087molecular_functionprotein-folding chaperone binding
B0060056biological_processmammary gland involution
B0061762biological_processCAMKK-AMPK signaling cascade
B0065003biological_processprotein-containing complex assembly
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CU A 1101
ChainResidue
AHIS162
AHIS974
AHIS1014
AHOH1209

site_idAC2
Number of Residues5
Detailsbinding site for residue CU A 1102
ChainResidue
ALEU968
AHIS969
ACYS1015
AHIS1020
AMET1025

site_idAC3
Number of Residues5
Detailsbinding site for residue CU A 1103
ChainResidue
AHIS275
ACYS318
AASN320
AHIS323
ALEU328

site_idAC4
Number of Residues4
Detailsbinding site for residue CU A 1104
ChainResidue
AHIS103
AHIS160
AHIS1016
AHOH1209

site_idAC5
Number of Residues5
Detailsbinding site for residue CU A 1105
ChainResidue
AHIS101
AALA102
AHIS103
AHIS972
AHIS974

site_idAC6
Number of Residues6
Detailsbinding site for residue CA A 1106
ChainResidue
ALYS109
AGLU112
AASP118
AGLN124
AASP127
AASP128

site_idAC7
Number of Residues4
Detailsbinding site for residue NA A 1107
ChainResidue
ATYR36
AGLY45
ATYR48
ASER236

site_idAC8
Number of Residues6
Detailsbinding site for residue CU B 1101
ChainResidue
BLEU968
BHIS969
BCYS1015
BVAL1017
BHIS1020
BMET1025

site_idAC9
Number of Residues5
Detailsbinding site for residue CU B 1102
ChainResidue
BHIS275
BCYS318
BASN320
BHIS323
BLEU328

site_idAD1
Number of Residues4
Detailsbinding site for residue CU B 1103
ChainResidue
BHIS103
BHIS160
BHIS1016
BCU1106

site_idAD2
Number of Residues6
Detailsbinding site for residue CU B 1104
ChainResidue
BVAL630
BHIS631
BCYS674
BTHR676
BHIS679
BMET684

site_idAD3
Number of Residues5
Detailsbinding site for residue CU B 1105
ChainResidue
BHIS162
BHIS974
BHIS1014
BHIS1016
BCU1106

site_idAD4
Number of Residues5
Detailsbinding site for residue CU B 1106
ChainResidue
BHIS101
BHIS103
BHIS972
BCU1103
BCU1105

site_idAD5
Number of Residues5
Detailsbinding site for residue CA B 1107
ChainResidue
BLYS109
BASP118
BGLN124
BASP127
BASP128

site_idAD6
Number of Residues4
Detailsbinding site for residue NA B 1108
ChainResidue
BTYR36
BGLY45
BTYR48
BSER236

Functional Information from PROSITE/UniProt
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GvWmLsCqNLnhLkAGLqafF
ChainResidueDetails
AGLY312-PHE332
AGLY668-TYR688
AGLY1009-TYR1029

site_idPS00080
Number of Residues12
DetailsMULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM
ChainResidueDetails
AHIS1014-MET1025

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI4
Number of Residues358
DetailsDomain: {"description":"Plastocyanin-like 1","evidences":[{"source":"UniProtKB","id":"P00450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues296
DetailsDomain: {"description":"Plastocyanin-like 2","evidences":[{"source":"UniProtKB","id":"P00450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues370
DetailsDomain: {"description":"Plastocyanin-like 3","evidences":[{"source":"UniProtKB","id":"P00450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues296
DetailsDomain: {"description":"Plastocyanin-like 4","evidences":[{"source":"UniProtKB","id":"P00450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues340
DetailsDomain: {"description":"Plastocyanin-like 5","evidences":[{"source":"UniProtKB","id":"P00450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsActive site: {"description":"Nucleophile; for glutathione peroxidase activity","evidences":[{"source":"UniProtKB","id":"P00450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues42
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues6
DetailsBinding site: {"description":"type 3 copper site","evidences":[{"source":"UniProtKB","id":"P00450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues22
DetailsBinding site: {"description":"type 1 copper site","evidences":[{"source":"UniProtKB","id":"P00450","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues12
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon