Literature summary for 2.6.1.52 extracted from

Battula, P.; Dubnovitsky, A.P.; Papageorgiou, A.C.
Structural basis of L-phosphoserine binding to Bacillus alcalophilus phosphoserine aminotransferase (2013), Acta Crystallogr. Sect. D, 69, 804-811.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
in presence or absence of L-phosphoserine, to resolutions of 1.5 and 1.6 A, respectively. Substrate binding induces local conformational changes. No domain or subunit movements are observed. Residues Arg42 and Arg328 and His41 and His327 form a tight binding site for the phosphate group of L-phosphoserine	Alkalihalobacillus alcalophilus

Organism

Organism	UniProt	Comment	Textmining
Alkalihalobacillus alcalophilus	Q9RME2	-	-

Synonyms

Synonyms	Comment	Organism
serC	-	Alkalihalobacillus alcalophilus

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Release 2023.1 (January 2023)