Ligand id: 5151

Name: bestatin

Structure and Physico-chemical Properties

2D Structure
Calculated Physico-chemical Properties
Hydrogen bond acceptors 6
Hydrogen bond donors 4
Rotatable bonds 9
Topological polar surface area 112.65
Molecular weight 308.17
XLogP -0.92
No. Lipinski's rules broken 0

Molecular properties generated using the CDK

1. Grembecka J, Mucha A, Cierpicki T, Kafarski P. (2003)
The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity.
J. Med. Chem., 46 (13): 2641-55. [PMID:12801228]
2. Orning L, Krivi G, Fitzpatrick FA. (1991)
Leukotriene A4 hydrolase. Inhibition by bestatin and intrinsic aminopeptidase activity establish its functional resemblance to metallohydrolase enzymes.
J. Biol. Chem., 266 (3): 1375-8. [PMID:1846352]
3. Taylor A, Peltier CZ, Torre FJ, Hakamian N. (1993)
Inhibition of bovine lens leucine aminopeptidase by bestatin: number of binding sites and slow binding of this inhibitor.
Biochemistry, 32 (3): 784-90. [PMID:8422382]