Literature summary for 3.1.1.1 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.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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

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

Subunits

Subunits	Comment	Organism
dimer	crystallization data	unidentified

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Release 2023.1 (January 2023)