Literature summary extracted from

Byun, J.; Rhee, J.; Kim, N.D.; Yoon, J.; Kim, D.; Koh, E.; Oh, J.; Cho, H.
Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties (2007), BMC Struct. Biol., 7, 2007.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
3.1.1.1	at 2.1 A resolution. Enzyme exhibits a classical alpha/beta hydrolase fold with a central parallel-stranded beta sheet surrounded by alpha helices on both sides. The catalytic motif is formed by residues S154, D251, and H281. Enzyme forms a dimer via hydrophobic interactions through residues V274 and F276 on the beta strand off each monomer, and via salt bridges	unidentified

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.1.1.1	unidentified	-	isoform EstE1, organism isolated from a thermal environmental sample	-

Subunits

EC Number	Subunits	Comment	Organism
3.1.1.1	dimer	crystallization data	unidentified

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Release 2023.1 (January 2023)