Literature summary for 3.1.2.2 extracted from

Cheng, F.; Wang, Q.; Chen, M.; Quiocho, F.A.; Ma, J.
Molecular docking study of the interactions between the thioesterase domain of human fatty acid synthase and its ligands (2008), Proteins Struct. Funct. Bioinform., 70, 1228-1234.

Crystallization (Commentary)

Crystallization (Comment)	Organism
docking studies to the pocket of the catalytic triad Ser 2308, His 2481, and Asp 2338, using palmitate, and fatty acids with chain lengths of 12 to 20 carbon atoms. The ligand binding pocket of the thioesterase domain is a decisive factor in chain length specificity. Binding of palmitate results in the most favorable binding free enrgy among the fatty acids tested. The experimentally amino acids of the catalytic triad Ser2308, His2481, and Asp2338 are located very close to the carboxyl group of palmitate. The close location of Arg2482 to the carboxyl group of palmitate and the catalytic triad implies an important role of this residue in catalysis	Homo sapiens

Crystallization (Comment)

Organism

docking studies to the pocket of the catalytic triad Ser 2308, His 2481, and Asp 2338, using palmitate, and fatty acids with chain lengths of 12 to 20 carbon atoms. The ligand binding pocket of the thioesterase domain is a decisive factor in chain length specificity. Binding of palmitate results in the most favorable binding free enrgy among the fatty acids tested. The experimentally amino acids of the catalytic triad Ser2308, His2481, and Asp2338 are located very close to the carboxyl group of palmitate. The close location of Arg2482 to the carboxyl group of palmitate and the catalytic triad implies an important role of this residue in catalysis

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
C75	docking studies. C75 binds the thioestrase domain in a similar orientation to that of palmitate, with its hydrophobic group buried inside the distal pocket and hydrophilic group interacting with the catalytic triad	Homo sapiens
orlistat	docking studies, high binding affinity for the thioesterase domain	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	docking studies to the pocket of the catalytic triad Ser 2308, His 2481, and Asp 2338, using palmitate, and fatty acids with chain lengths of 12 to 20 carbon atoms. The ligand binding pocket of the thioesterase domain is a decisive factor in chain length specificity. Binding of palmitate results in the most favorable binding free enrgy among the fatty acids tested. The experimentally amino acids of the catalytic triad Ser2308, His2481, and Asp2338 are located very close to the carboxyl group of palmitate. The close location of Arg2482 to the carboxyl group of palmitate and the catalytic triad implies an important role of this residue in catalysis	Homo sapiens	?	-	?