Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2-(2-carboxy-4-nitro-phenyl) disulfonyl-5-nitrobenzoic acid | i.e. NSC517871. Molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored | Homo sapiens | |
2-nitro-5-sulfo-sulfonyl-benzoic acid | molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored | Homo sapiens | |
2-Nitro-5-thiocyanobenzoic acid | molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored | Homo sapiens | |
5-(3-carboxy-4-nitro-phenyl) sulfonyl-2-nitrobenzoic acid | i.e. NSC695265. Molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored | Homo sapiens | |
Dithionitrobenzoic acid | molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored | Homo sapiens | |
thionitrobenzoic acid | molecular docking simulation into the redox-active site, residues C37, G38, H39, C40. Inhibitor binds to hydrophobic amino acidsA34, W36, C37, C40, H39, T68 and F80. The redox inhibitory conformations are energetically and statistically favored | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P07237 | - |
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