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X-RAY CRYSTAL STRUCTURE OF HUMAN CERULOPLASMIN AT 3.0 ANGSTROMS
Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0005765 | cellular_component | lysosomal membrane |
A | 0005788 | cellular_component | endoplasmic reticulum lumen |
A | 0005886 | cellular_component | plasma membrane |
A | 0006811 | biological_process | monoatomic ion transport |
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 | 0016491 | molecular_function | oxidoreductase activity |
A | 0016724 | molecular_function | oxidoreductase activity, acting on metal ions, oxygen as acceptor |
A | 0038023 | molecular_function | signaling receptor activity |
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 | 0070062 | cellular_component | extracellular exosome |
A | 0072562 | cellular_component | blood microparticle |
A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
site_id | CU1 |
Number of Residues | 5 |
Details | TYPE I CU BINDING SITE IN DOMAIN 2. AT BEST LEU 329 MAY HAVE VAN DER WAALS CONTACT WITH THE CU. |
Chain | Residue |
A | CU1049 |
A | HIS276 |
A | CYS319 |
A | HIS324 |
A | LEU329 |
site_id | CU2 |
Number of Residues | 5 |
Details | TYPE I CU BINDING SITE IN DOMAIN 4. |
Chain | Residue |
A | MET690 |
A | CU1053 |
A | HIS637 |
A | CYS680 |
A | HIS685 |
site_id | CU3 |
Number of Residues | 5 |
Details | LABILE CU BINDING SITE IN DOMAIN 4. |
Chain | Residue |
A | CU1054 |
A | GLU597 |
A | HIS602 |
A | ASP684 |
A | GLU971 |
site_id | CU4 |
Number of Residues | 5 |
Details | TYPE I CU BINDING SITE IN DOMAIN 6. |
Chain | Residue |
A | CU1055 |
A | HIS975 |
A | CYS1021 |
A | HIS1026 |
A | MET1031 |
site_id | CU5 |
Number of Residues | 5 |
Details | LABILE CU BINDING SITE IN DOMAIN 6. |
Chain | Residue |
A | CU1056 |
A | GLU272 |
A | GLU935 |
A | HIS940 |
A | ASP1025 |
site_id | TRI |
Number of Residues | 13 |
Details | TRINUCLEAR CENTER. CU31 AND 32 ARE THE PAIR OF TYPE III CU AND CU34 IS THE TYPE II CU. O33 BRIDGES CU 31 - 32 AND O35 BRIDGES Y 107 - CU 34. |
Chain | Residue |
A | CU1050 |
A | CU1051 |
A | O1057 |
A | CU1052 |
A | O1058 |
A | HIS101 |
A | HIS103 |
A | HIS161 |
A | HIS163 |
A | HIS978 |
A | HIS980 |
A | HIS1020 |
A | HIS1022 |
Functional Information from PROSITE/UniProt
site_id | PS00079 |
Number of Residues | 21 |
Details | MULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GeWmLsCqNLnhLkAGLqafF |
Chain | Residue | Details |
A | GLY313-PHE333 | |
A | GLY674-TYR694 | |
A | GLY1015-TYR1035 |
site_id | PS00080 |
Number of Residues | 12 |
Details | MULTICOPPER_OXIDASE2 Multicopper oxidases signature 2. HCHvtdHihaGM |
Chain | Residue | Details |
A | HIS1020-MET1031 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: type 2 copper site |
Chain | Residue | Details |
A | HIS101 | |
A | HIS978 |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: type 3 copper site |
Chain | Residue | Details |
A | HIS103 | |
A | HIS161 | |
A | HIS163 | |
A | HIS980 | |
A | HIS1020 | |
A | HIS1022 |
site_id | SWS_FT_FI3 |
Number of Residues | 11 |
Details | BINDING: type 1 copper site |
Chain | Residue | Details |
A | HIS276 | |
A | HIS1026 | |
A | MET1031 | |
A | CYS319 | |
A | HIS324 | |
A | HIS637 | |
A | CYS680 | |
A | HIS685 | |
A | MET690 | |
A | HIS975 | |
A | CYS1021 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039 |
Chain | Residue | Details |
A | SER703 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169 |
Chain | Residue | Details |
A | ASN119 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169 |
Chain | Residue | Details |
A | ASN339 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169 |
Chain | Residue | Details |
A | ASN378 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952 |
Chain | Residue | Details |
A | ASN569 | |
A | ASN907 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218 |
Chain | Residue | Details |
A | ASN743 |