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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_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile; for glutathione peroxidase activity => ECO:0000250|UniProtKB:P00450
ChainResidueDetails
ACYS674
BCYS674

site_idSWS_FT_FI2
Number of Residues42
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00450
ChainResidueDetails
ATYR36
ASER236
APHE388
AGLY397
ATYR400
ASER592
APHE742
AGLY751
ATYR754
ASER930
AHIS972
AGLY45
AHIS974
AHIS1016
BTYR36
BGLY45
BTYR48
BHIS101
BLYS109
BGLN124
BASP127
BASP128
ATYR48
BHIS160
BSER236
BPHE388
BGLY397
BTYR400
BSER592
BPHE742
BGLY751
BTYR754
BSER930
AHIS101
BHIS972
BHIS974
BHIS1016
ALYS109
AGLN124
AASP127
AASP128
AHIS160

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: type 3 copper site => ECO:0000250|UniProtKB:P00450
ChainResidueDetails
AHIS103
AHIS162
AHIS1014
BHIS103
BHIS162
BHIS1014

site_idSWS_FT_FI4
Number of Residues22
DetailsBINDING: type 1 copper site => ECO:0000250|UniProtKB:P00450
ChainResidueDetails
AHIS275
AHIS1020
AMET1025
BHIS275
BCYS318
BHIS323
BHIS631
BCYS674
BHIS679
BMET684
BHIS969
ACYS318
BCYS1015
BHIS1020
BMET1025
AHIS323
AHIS631
ACYS674
AHIS679
AMET684
AHIS969
ACYS1015

site_idSWS_FT_FI5
Number of Residues12
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN119
BASN563
BASN737
BASN901
AASN207
AASN377
AASN563
AASN737
AASN901
BASN119
BASN207
BASN377

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PDB entries from 2025-06-11

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