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Literature summary for 5.3.4.1 extracted from

  • Gowthaman, U.; Jayakanthan, M.; Sundar, D.
    Molecular docking studies of dithionitrobenzoic acid and its related compounds to protein disulfide isomerase: computational screening of inhibitors to HIV-1 entry (2008), BMC Bioinformatics, 9 Suppl 12, S14.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

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

Organism UniProt Comment Textmining
Homo sapiens P07237
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