Click to view 3D structure | 3-isopropylmalate dehydrogenase | Q5SIY4 | Thermus thermophilus | Predicted (SEA) | 0.233548 |
Click to view 3D structure | Free fatty acid receptor 3 | B2GV46 | Rattus norvegicus | Predicted (SEA) | 1.08989 |
Click to view 3D structure | Carbonic anhydrase 9 | Q16790 | Humans | Predicted (SEA) | 4846.43 |
Click to view 3D structure | Fumarate hydratase, mitochondrial | P10173 | Sus scrofa | Predicted (SEA) | 1.40129 |
Click to view 3D structure | Alpha carbonic anhydrase | B5SU02 | Stylophora pistillata | Predicted (SEA) | 443.818 |
Click to view 3D structure | Egl nine homolog 1 | Q9GZT9 | Humans | Predicted (SEA) | 3560.67 |
Click to view 3D structure | Olfactory receptor 51E2 | Q9H255 | Humans | Predicted (SEA) | 53.2489 |
Click to view 3D structure | Beta-lactamase VIM-1 | Q9XAY4 | Pseudomonas aeruginosa | Predicted (SEA) | 9.809 |
Click to view 3D structure | Carbonic anhydrase 1 | P00915 | Humans | Predicted (SEA) | 6790.71 |
Click to view 3D structure | Asc-type amino acid transporter 1 | P63116 | Rat | Predicted (SEA) | 35.5771 |
Click to view 3D structure | Sodium- and chloride-dependent GABA transporter 2 | P31646 | Rattus norvegicus | Predicted (SEA) | 59.399 |
Click to view 3D structure | Carbonic anhydrase 4 | P22748 | Humans | Predicted (SEA) | 6601.3 |
Click to view 3D structure | Carbonic anhydrase 2 | P00918 | Humans | Predicted (SEA) | 7483.49 |
Click to view 3D structure | Carbonic anhydrase 7 | P43166 | Humans | Predicted (SEA) | 7057.34 |
Click to view 3D structure | Carbonic anhydrase 12 | O43570 | Humans | Predicted (SEA) | 7386.1 |
Click to view 3D structure | Carbonic anhydrase 6 | P23280 | Humans | Predicted (SEA) | 6814.61 |
Click to view 3D structure | Carbonic anhydrase 14 | Q9ULX7 | Humans | Predicted (SEA) | 6890.28 |
Click to view 3D structure | Carnitine O-palmitoyltransferase 2, mitochondrial | P23786 | Humans | Predicted (SEA) | 4633.66 |
Click to view 3D structure | Cocaine esterase | O00748 | Humans | Predicted (SEA) | 5012.71 |
Click to view 3D structure | Liver carboxylesterase 1 | P23141 | Humans | Predicted (SEA) | 4944.44 |
Click to view 3D structure | Lysine-specific demethylase 5C | P41229 | Humans | Predicted (SEA) | 6512.4 |
Click to view 3D structure | Carbonic anhydrase 4 | Q95323 | Bos taurus | Predicted (SEA) | 4837.78 |
Click to view 3D structure | Carbonic anhydrase 5B, mitochondrial | Q9Y2D0 | Humans | Predicted (SEA) | 7145.86 |
Click to view 3D structure | Carbonic anhydrase 5A, mitochondrial | P35218 | Humans | Predicted (SEA) | 7287.47 |
Click to view 3D structure | Carbonic anhydrase 15 | Q99N23 | Mus musculus | Predicted (SEA) | 6572.11 |
Click to view 3D structure | Glucose-6-phosphate 1-dehydrogenase | P11413 | Humans | Known | Excess copper is sequestered within hepatocyte lysosomes, where it is complexed with metallothionein. Copper hepatotoxicity is believed to occur when the lysosomes become saturated and copper accumulates in the nucleus, causing nuclear damage. This damage is possibly a result of oxidative damage, including lipid peroxidation. Copper inhibits the sulfhydryl group enzymes such as glucose-6-phosphate 1-dehydrogenase, glutathione reductase, and paraoxonases, which protect the cell from free oxygen radicals. It also influences gene expression and is a co-factor for oxidative enzymes such as cytochrome C oxidase and lysyl oxidase. In addition, the oxidative stress induced by copper is thought to activate acid sphingomyelinase, which lead to the production of ceramide, an apoptotic signal, as well as cause hemolytic anemia. (L277, T49, A174, L280) |
Click to view 3D structure | Glutathione reductase, mitochondrial | P00390 | Humans | Known | Excess copper is sequestered within hepatocyte lysosomes, where it is complexed with metallothionein. Copper hepatotoxicity is believed to occur when the lysosomes become saturated and copper accumulates in the nucleus, causing nuclear damage. This damage is possibly a result of oxidative damage, including lipid peroxidation. Copper inhibits the sulfhydryl group enzymes such as glucose-6-phosphate 1-dehydrogenase, glutathione reductase, and paraoxonases, which protect the cell from free oxygen radicals. It also influences gene expression and is a co-factor for oxidative enzymes such as cytochrome C oxidase and lysyl oxidase. In addition, the oxidative stress induced by copper is thought to activate acid sphingomyelinase, which lead to the production of ceramide, an apoptotic signal, as well as cause hemolytic anemia. (L277, T49, A174, L280) |
Click to view 3D structure | Serum paraoxonase/arylesterase 1 | P27169 | Humans | Known | Excess copper is sequestered within hepatocyte lysosomes, where it is complexed with metallothionein. Copper hepatotoxicity is believed to occur when the lysosomes become saturated and copper accumulates in the nucleus, causing nuclear damage. This damage is possibly a result of oxidative damage, including lipid peroxidation. Copper inhibits the sulfhydryl group enzymes such as glucose-6-phosphate 1-dehydrogenase, glutathione reductase, and paraoxonases, which protect the cell from free oxygen radicals. It also influences gene expression and is a co-factor for oxidative enzymes such as cytochrome C oxidase and lysyl oxidase. In addition, the oxidative stress induced by copper is thought to activate acid sphingomyelinase, which lead to the production of ceramide, an apoptotic signal, as well as cause hemolytic anemia. (L277, T49, A174, L280) |
Click to view 3D structure | Serum paraoxonase/lactonase 3 | Q15166 | Humans | Known | Excess copper is sequestered within hepatocyte lysosomes, where it is complexed with metallothionein. Copper hepatotoxicity is believed to occur when the lysosomes become saturated and copper accumulates in the nucleus, causing nuclear damage. This damage is possibly a result of oxidative damage, including lipid peroxidation. Copper inhibits the sulfhydryl group enzymes such as glucose-6-phosphate 1-dehydrogenase, glutathione reductase, and paraoxonases, which protect the cell from free oxygen radicals. It also influences gene expression and is a co-factor for oxidative enzymes such as cytochrome C oxidase and lysyl oxidase. In addition, the oxidative stress induced by copper is thought to activate acid sphingomyelinase, which lead to the production of ceramide, an apoptotic signal, as well as cause hemolytic anemia. (L277, T49, A174, L280) |
Click to view 3D structure | Alpha-synuclein | P37840 | Humans | Known | Copper binds to alpha-synuclein, initiating protein aggregation and likely contributing to the development of the neurodegenerative disorders Parkinson's disease and Alzheimer's disease. (A173) |
Click to view 3D structure | Amyloid-beta precursor protein | P05067 | Humans | Known | Copper binds the N-terminal region of amyloid precursor protein, promoting the generation of _-amyloid from the protein. This is believed to contribute to the development of the neurodegenerative disorders Parkinson's disease and Alzheimer's disease. (A173) |