5N4L
Rat ceruloplasmin trigonal form
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001889 | biological_process | liver development |
| 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 | 0005886 | cellular_component | plasma membrane |
| A | 0006825 | biological_process | copper ion transport |
| A | 0006826 | biological_process | iron ion transport |
| A | 0006878 | biological_process | intracellular copper ion homeostasis |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0007565 | biological_process | female pregnancy |
| A | 0007584 | biological_process | response to nutrient |
| A | 0007595 | biological_process | lactation |
| A | 0009986 | cellular_component | cell surface |
| A | 0015679 | biological_process | plasma membrane copper ion transport |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016724 | molecular_function | oxidoreductase activity, acting on metal ions, oxygen as acceptor |
| A | 0030324 | biological_process | lung development |
| A | 0046688 | biological_process | response to copper ion |
| 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 | 0060056 | biological_process | mammary gland involution |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0001889 | biological_process | liver development |
| B | 0004322 | molecular_function | ferroxidase activity |
| B | 0004602 | molecular_function | glutathione peroxidase activity |
| B | 0005507 | molecular_function | copper ion binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006825 | biological_process | copper ion transport |
| B | 0006826 | biological_process | iron ion transport |
| B | 0006878 | biological_process | intracellular copper ion homeostasis |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0007565 | biological_process | female pregnancy |
| B | 0007584 | biological_process | response to nutrient |
| B | 0007595 | biological_process | lactation |
| B | 0009986 | cellular_component | cell surface |
| B | 0015679 | biological_process | plasma membrane copper ion transport |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016724 | molecular_function | oxidoreductase activity, acting on metal ions, oxygen as acceptor |
| B | 0030324 | biological_process | lung development |
| B | 0046688 | biological_process | response to copper ion |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0047066 | molecular_function | phospholipid-hydroperoxide glutathione peroxidase activity |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0060056 | biological_process | mammary gland involution |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 1101 |
| Chain | Residue |
| A | HIS162 |
| A | HIS974 |
| A | HIS1014 |
| A | HOH1209 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CU A 1102 |
| Chain | Residue |
| A | LEU968 |
| A | HIS969 |
| A | CYS1015 |
| A | HIS1020 |
| A | MET1025 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue CU A 1103 |
| Chain | Residue |
| A | HIS275 |
| A | CYS318 |
| A | ASN320 |
| A | HIS323 |
| A | LEU328 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CU A 1104 |
| Chain | Residue |
| A | HIS103 |
| A | HIS160 |
| A | HIS1016 |
| A | HOH1209 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CU A 1105 |
| Chain | Residue |
| A | HIS101 |
| A | ALA102 |
| A | HIS103 |
| A | HIS972 |
| A | HIS974 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 1106 |
| Chain | Residue |
| A | LYS109 |
| A | GLU112 |
| A | ASP118 |
| A | GLN124 |
| A | ASP127 |
| A | ASP128 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 1107 |
| Chain | Residue |
| A | TYR36 |
| A | GLY45 |
| A | TYR48 |
| A | SER236 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue CU B 1101 |
| Chain | Residue |
| B | LEU968 |
| B | HIS969 |
| B | CYS1015 |
| B | VAL1017 |
| B | HIS1020 |
| B | MET1025 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue CU B 1102 |
| Chain | Residue |
| B | HIS275 |
| B | CYS318 |
| B | ASN320 |
| B | HIS323 |
| B | LEU328 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue CU B 1103 |
| Chain | Residue |
| B | HIS103 |
| B | HIS160 |
| B | HIS1016 |
| B | CU1106 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CU B 1104 |
| Chain | Residue |
| B | VAL630 |
| B | HIS631 |
| B | CYS674 |
| B | THR676 |
| B | HIS679 |
| B | MET684 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue CU B 1105 |
| Chain | Residue |
| B | HIS162 |
| B | HIS974 |
| B | HIS1014 |
| B | HIS1016 |
| B | CU1106 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue CU B 1106 |
| Chain | Residue |
| B | HIS101 |
| B | HIS103 |
| B | HIS972 |
| B | CU1103 |
| B | CU1105 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue CA B 1107 |
| Chain | Residue |
| B | LYS109 |
| B | ASP118 |
| B | GLN124 |
| B | ASP127 |
| B | ASP128 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 1108 |
| Chain | Residue |
| B | TYR36 |
| B | GLY45 |
| B | TYR48 |
| B | SER236 |
Functional Information from PROSITE/UniProt
| site_id | PS00079 |
| Number of Residues | 21 |
| Details | MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GvWmLsCqNLnhLkAGLqafF |
| Chain | Residue | Details |
| A | GLY312-PHE332 | |
| A | GLY668-TYR688 | |
| A | GLY1009-TYR1029 |
| site_id | PS00080 |
| Number of Residues | 12 |
| Details | MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM |
| Chain | Residue | Details |
| A | HIS1014-MET1025 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile; for glutathione peroxidase activity => ECO:0000250|UniProtKB:P00450 |
| Chain | Residue | Details |
| A | CYS674 | |
| B | CYS674 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00450 |
| Chain | Residue | Details |
| A | TYR36 | |
| A | GLY397 | |
| A | TYR400 | |
| A | SER592 | |
| A | PHE742 | |
| A | GLY751 | |
| A | TYR754 | |
| A | SER930 | |
| B | TYR36 | |
| B | GLY45 | |
| B | TYR48 | |
| A | GLY45 | |
| B | LYS109 | |
| B | GLN124 | |
| B | ASP127 | |
| B | ASP128 | |
| B | SER236 | |
| B | PHE388 | |
| B | GLY397 | |
| B | TYR400 | |
| B | SER592 | |
| B | PHE742 | |
| A | TYR48 | |
| B | GLY751 | |
| B | TYR754 | |
| B | SER930 | |
| A | LYS109 | |
| A | GLN124 | |
| A | ASP127 | |
| A | ASP128 | |
| A | SER236 | |
| A | PHE388 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: type 2 copper site => ECO:0000250|UniProtKB:P00450 |
| Chain | Residue | Details |
| A | HIS101 | |
| A | HIS972 | |
| B | HIS101 | |
| B | HIS972 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: type 3 copper site => ECO:0000250|UniProtKB:P00450 |
| Chain | Residue | Details |
| A | HIS103 | |
| B | HIS974 | |
| B | HIS1014 | |
| B | HIS1016 | |
| A | HIS160 | |
| A | HIS162 | |
| A | HIS974 | |
| A | HIS1014 | |
| A | HIS1016 | |
| B | HIS103 | |
| B | HIS160 | |
| B | HIS162 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | BINDING: type 1 copper site => ECO:0000250|UniProtKB:P00450 |
| Chain | Residue | Details |
| A | HIS275 | |
| A | HIS1020 | |
| A | MET1025 | |
| B | HIS275 | |
| B | CYS318 | |
| B | HIS323 | |
| B | HIS631 | |
| B | CYS674 | |
| B | HIS679 | |
| B | MET684 | |
| B | HIS969 | |
| A | CYS318 | |
| B | CYS1015 | |
| B | HIS1020 | |
| B | MET1025 | |
| A | HIS323 | |
| A | HIS631 | |
| A | CYS674 | |
| A | HIS679 | |
| A | MET684 | |
| A | HIS969 | |
| A | CYS1015 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| A | ASN119 | |
| B | ASN563 | |
| B | ASN737 | |
| B | ASN901 | |
| A | ASN207 | |
| A | ASN377 | |
| A | ASN563 | |
| A | ASN737 | |
| A | ASN901 | |
| B | ASN119 | |
| B | ASN207 | |
| B | ASN377 |
