Literature summary for 2.3.1.129 extracted from

Ngo, A.; Fong, K.T.; Cox, D.L.; Chen, X.; Fisher, A.J.
Structures of Bacteroides fragilis uridine 5-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA) (2015), Acta Crystallogr. Sect. D, 71, 1068-1076.

Search for more literature for 2.3.1.129

Cloned(Commentary)

Cloned (Comment)	Organism
-	Bacteroides fragilis

Crystallization (Commentary)

Crystallization (Comment)	Organism
structures of ligand-free and UDP-GlcNAc-bound enzyme. The enzyme crystallizes in a cubic space group, with the crystallographic threefold axis generating the biological functional homotrimer and with each monomer forming a nine-ring left-handed beta-helical fold in the N-terminus followed by an alpha-helical motif in the C-terminus. Calcium ions are observed on the threefold axis to help stabilize the trimeric assembly	Bacteroides fragilis

Crystallization (Comment)

Organism

structures of ligand-free and UDP-GlcNAc-bound enzyme. The enzyme crystallizes in a cubic space group, with the crystallographic threefold axis generating the biological functional homotrimer and with each monomer forming a nine-ring left-handed beta-helical fold in the N-terminus followed by an alpha-helical motif in the C-terminus. Calcium ions are observed on the threefold axis to help stabilize the trimeric assembly

Bacteroides fragilis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	calcium ions are observed on the threefold axis to help stabilize the trimeric assembly, crystallization data	Bacteroides fragilis

Organism

Organism	UniProt	Comment	Textmining
Bacteroides fragilis	Q5LH16	-	-
Bacteroides fragilis DSM 2151	Q5LH16	-	-

Synonyms

Synonyms	Comment	Organism
LpxA	-	Bacteroides fragilis

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Release 2023.1 (January 2023)