EC Number   |
|---|
    1.13.11.34 | - |
| 1.13.11.34 | crystal structure analysis |
| 1.13.11.34 | in complex with inhibitor nordihydroguaiaretic acid, at 2.71 A resolution. The presence of the inhibitor is incompatible with the closed structure of the enzyme. Structure in complex with inhibitor 3-acetyl-11-keto-beta-boswellic acid at 3.0 A resolution. 3-Acetyl-11-keto-beta-boswellic acid lies lengthwise in a deep groove between the amino-terminal and catalytic domains |
| 1.13.11.34 | molecular docking of inhibitor delta-garcinoic acid. Trp102 within the allosteric binding site is important for binding. There is an intermolecular hydrogen bond between the ligand's phenolic oxygen and the NH of the indole of Trp102 and one links the amide function of Val110's backbone and the ligand's carbonyl group. The phytyl-like side chain and both methyl substituents of the chromanol form hydrophobic interactions with Val110, His130, Lys133, Tyr383, and Arg401 |
| 1.13.11.34 | molecular docking of inhibitor ferrocenyl carboxylic acid. The carboxylate group of the ferrocenyl complex may be oriented towards the catalytic site of the enzyme or may be located at the cavity entrance of the active site |
