2.3.1.46: homoserine O-succinyltransferase
This is an abbreviated version!
For detailed information about homoserine O-succinyltransferase, go to the full flat file.
Word Map on EC 2.3.1.46
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2.3.1.46
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chaperone
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acyltransferases
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refolding
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noncanonical
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cereus
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threonine
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biotechnology
- 2.3.1.46
- chaperone
- acyltransferases
-
refolding
-
noncanonical
- cereus
- threonine
- biotechnology
Reaction
Synonyms
homoserine O-succinyltransferase, homoserine O-transsuccinylase, homoserine succinyltransferase, homoserine transsuccinylase, homoserine-O-succinyltransferase, HST, HTS, MetA, MetA protein, succinyltransferase, homoserine
ECTree
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Crystallization
Crystallization on EC 2.3.1.46 - homoserine O-succinyltransferase
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crystal structure of HTS from Bacillus cereus is determined to 2.4 A resolution. HTS is a single-domain protein with a Rossmann fold topology. The core of the protein is a parallel beta-sheet sandwiched by alpha-helices. HTS is composed of 11 beta-strands, 7 alpha-helices, and four 310-helices