7XUM
Structure of ATP7B C983S/C985S/D1027A mutant with Cu+ in presence of ATOX1
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000139 | cellular_component | Golgi membrane |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005215 | molecular_function | transporter activity |
A | 0005375 | molecular_function | copper ion transmembrane transporter activity |
A | 0005507 | molecular_function | copper ion binding |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005768 | cellular_component | endosome |
A | 0005770 | cellular_component | late endosome |
A | 0005794 | cellular_component | Golgi apparatus |
A | 0005802 | cellular_component | trans-Golgi network |
A | 0005886 | cellular_component | plasma membrane |
A | 0006812 | biological_process | monoatomic cation transport |
A | 0006825 | biological_process | copper ion transport |
A | 0006878 | biological_process | intracellular copper ion homeostasis |
A | 0006882 | biological_process | intracellular zinc ion homeostasis |
A | 0007595 | biological_process | lactation |
A | 0015677 | biological_process | copper ion import |
A | 0015680 | biological_process | protein maturation by copper ion transfer |
A | 0016020 | cellular_component | membrane |
A | 0016323 | cellular_component | basolateral plasma membrane |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0019829 | molecular_function | ATPase-coupled monoatomic cation transmembrane transporter activity |
A | 0031410 | cellular_component | cytoplasmic vesicle |
A | 0032588 | cellular_component | trans-Golgi network membrane |
A | 0034220 | biological_process | monoatomic ion transmembrane transport |
A | 0035434 | biological_process | copper ion transmembrane transport |
A | 0043682 | molecular_function | P-type divalent copper transporter activity |
A | 0046688 | biological_process | response to copper ion |
A | 0046872 | molecular_function | metal ion binding |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0051208 | biological_process | sequestering of calcium ion |
A | 0051649 | biological_process | establishment of localization in cell |
A | 0060003 | biological_process | copper ion export |
A | 0140581 | molecular_function | P-type monovalent copper transporter activity |
A | 1990961 | biological_process | xenobiotic detoxification by transmembrane export across the plasma membrane |
Functional Information from PROSITE/UniProt
site_id | PS01047 |
Number of Residues | 30 |
Details | HMA_1 Heavy-metal-associated domain. IlGMtCqSCvksIEdrIsnlkgiismk.VsL |
Chain | Residue | Details |
A | ILE64-LEU93 | |
A | VAL149-LEU178 | |
A | ILE263-LEU292 | |
A | ILE365-LEU394 | |
A | ILE494-LEU523 | |
A | ILE570-LEU599 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1211 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
A | MET1-SER653 | |
A | ALA718-HIS724 | |
A | SER786-ARG919 | |
A | VAL995-ARG1322 | |
A | GLN1372-ILE1465 |
site_id | SWS_FT_FI2 |
Number of Residues | 159 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
A | PHE654-SER675 | |
A | ILE698-GLN717 | |
A | ARG725-LEU745 | |
A | ASP765-LYS785 | |
A | PHE920-ILE942 | |
A | GLN973-ALA994 | |
A | ILE1323-ALA1340 | |
A | PRO1352-LEU1371 |
site_id | SWS_FT_FI3 |
Number of Residues | 78 |
Details | TOPO_DOM: Extracellular => ECO:0000255 |
Chain | Residue | Details |
A | ASN676-LEU697 | |
A | VAL746-PHE764 | |
A | GLY943-PHE972 | |
A | GLY1341-GLN1351 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | ACT_SITE: 4-aspartylphosphate intermediate => ECO:0000250 |
Chain | Residue | Details |
A | ALA1027 |
site_id | SWS_FT_FI5 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280, ECO:0000269|PubMed:18558714, ECO:0000269|PubMed:20032459 |
Chain | Residue | Details |
A | CYS69 | |
A | CYS72 | |
A | CYS154 | |
A | CYS157 | |
A | CYS268 | |
A | CYS271 | |
A | CYS370 | |
A | CYS373 | |
A | CYS499 | |
A | CYS502 | |
A | CYS575 | |
A | CYS578 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP1267 | |
A | ASP1271 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER23 | |
A | SER478 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q64535 |
Chain | Residue | Details |
A | SER481 | |
A | SER1398 |