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Literature summary for 6.3.2.9 extracted from

  • Perdih, A.; Bren, U.; Solmajer, T.
    Binding free energy calculations of N-sulphonyl-glutamic acid inhibitors of MurD ligase (2009), J. Mol. Model., 15, 983-996.
    View publication on PubMed
Search for more literature for 6.3.2.9

Inhibitors

Inhibitors Comment Organism Structure
(2R)-2-[[(7-(4-cyanobenzyloxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid calculation of binding free energies. Main driving force for binding are non-polar van der Waals-interactions Escherichia coli
(2R)-2-[[(7-benzyloxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid calculation of binding free energies. Main driving force for binding are non-polar van der Waals-interactions Escherichia coli
(2R)-2-[[(7-pentoxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid calculation of binding free energies. Main driving force for binding are non-polar van der Waals-interactions Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P14900
-
-

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.105
-
-
 Escherichia coli (2R)-2-[[(7-(4-cyanobenzyloxy)naphthalen-2-yl)sulfonyl]amino]pentanedioic acid
0.17
-
-
 Escherichia coli (2R)-2-[[(7-pentoxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid
0.239
-
-
 Escherichia coli (2R)-2-[[(7-benzyloxynaphthalen-2-yl)sulfonyl]amino]pentanedioic acid