Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the enzyme's heavy-metal binding domains may interact with the core of the proteins to achieve autoinhibition; the enzyme's heavy-metal binding domains may interact with the core of the proteins to achieve autoinhibition | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P35670 | ATP7B | - |
Homo sapiens | Q04656 | ATP7A | - |
Synonyms | Comment | Organism |
---|---|---|
ATP7A | - |
Homo sapiens |
ATP7B | - |
Homo sapiens |
copper P-type ATPase | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the P-type ATPases | Homo sapiens |
malfunction | enzyme missense mutations are involved in Menkes disease | Homo sapiens |
malfunction | enzyme missense mutations are involved in Wilson's disease | Homo sapiens |
additional information | the enzyme shows six sequential heavy-metal binding domains (HMBD1-HMBD6) and a type-specific constellation of transmembrane helices, the heavy-metal binding domains, HMBD5 and HMBD6 are the most crucial for function, the heavy-metal binding domains may interact with the core of the proteins to achieve autoinhibition. Homology structure modeling based on the existing structure of the soluble domain and the structure of the homologous LpCopA from the bacterium Legionella pneumophila. The domains and residues involved in the catalytic phosphorylation events and copper transfer are highly conserved | Homo sapiens |