Copper chaperone for superoxide dismutase

Summary

Copper chaperone for superoxide dismutase is a protein^[1].

Key Facts

• Copper chaperone for superoxide dismutase's instance of is recorded as protein^[2].
• Copper chaperone for superoxide dismutase's subclass of is recorded as protein^[3].
• Copper chaperone for superoxide dismutase's UniProt protein ID is recorded as O14618^[4].
• Copper chaperone for superoxide dismutase's part of is recorded as Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone^[5].
• Copper chaperone for superoxide dismutase's part of is recorded as Superoxide dismutase-like, copper/zinc binding domain superfamily^[6].
• Copper chaperone for superoxide dismutase's part of is recorded as Heavy metal-associated domain superfamily^[7].
• Copper chaperone for superoxide dismutase's part of is recorded as Heavy metal-associated domain, HMA, protein family^[8].
• Copper chaperone for superoxide dismutase's part of is recorded as Superoxide dismutase, copper/zinc binding domain, protein family^[9].
• Copper chaperone for superoxide dismutase's part of is recorded as Superoxide dismutase, copper/zinc, binding site, protein family^[10].
• Copper chaperone for superoxide dismutase's has part is recorded as Superoxide dismutase, copper/zinc, binding site^[11].
• Copper chaperone for superoxide dismutase's has part is recorded as Heavy metal-associated domain, HMA^[12].
• Copper chaperone for superoxide dismutase's has part is recorded as Superoxide dismutase, copper/zinc binding domain^[13].
• Copper chaperone for superoxide dismutase's RefSeq protein ID is recorded as NP_005116^[14].
• Copper chaperone for superoxide dismutase's PDB structure ID is recorded as 1DO5^[15].
• Copper chaperone for superoxide dismutase's PDB structure ID is recorded as 2CRL^[16].
• Copper chaperone for superoxide dismutase's PDB structure ID is recorded as 2RSQ^[17].
• Copper chaperone for superoxide dismutase's molecular function is recorded as protein-disulfide reductase activity^[18].
• Copper chaperone for superoxide dismutase's molecular function is recorded as zinc ion binding^[19].
• Copper chaperone for superoxide dismutase's molecular function is recorded as metal ion binding^[20].
• Copper chaperone for superoxide dismutase's molecular function is recorded as protein binding^[21].
• Copper chaperone for superoxide dismutase's molecular function is recorded as copper ion binding^[22].
• Copper chaperone for superoxide dismutase's molecular function is recorded as cadherin binding^[23].
• Copper chaperone for superoxide dismutase's molecular function is recorded as superoxide dismutase copper chaperone activity^[24].
• Copper chaperone for superoxide dismutase's molecular function is recorded as superoxide dismutase activity^[25].
• Copper chaperone for superoxide dismutase's molecular function is recorded as superoxide dismutase activity^[26].